Clinical Focus

  • Cancer > Urologic Oncology
  • Immunotherapy
  • Prostate Cancer
  • Medical Oncology
  • Genitourinary Cancer

Academic Appointments

Honors & Awards

  • Pilot Award, Stanford Translational Medicine Program (TRAM) (2012)
  • Fellowship Award, California Breast Cancer Research Program (2009-2010)
  • ASCO Young Investigator Award, American Society of Clinical Oncology (2009)
  • ASCO/AACR Workshop: Methods in Clinical Cancer Research, American Society of Clinical Oncology (2009)
  • NCCN Fellows Recognition Program, National Comprehensive Cancer Network (2007)
  • American Medical Association Seed Grant Award, American Medical Association (2002)
  • Howard Hughes Medical Institute Continuing Fellowship Award, Howard Hughes Medical Institute (2002)
  • Temple University Minority Research Trainee Forum Research Award, Temple University (2001-2)
  • UCSF Outstanding Performance Award, University of California, San Francisco (1996-8)

Professional Education

  • Fellowship:Stanford University - CAPS (2009) CA
  • Residency:Stanford University - CAPS (2005) CA
  • Medical Education:Univ Of Ws Sch Of Med-Madison (2003) WI
  • Board Certification: Internal Medicine, American Board of Internal Medicine (2007)

Research & Scholarship

Current Research and Scholarly Interests

Infiltration of specialized immune cells regulates the growth and survival of neoplasia. In a survey of leukocyte chemoattractant expression in public whole genome expression datasets, we found that the gene for chemerin is downregulated during tumorigenesis in animal models and in many human cancers. Low or absent chemerin expression predicted inferior outcomes in melanoma, and tumor-expressed chemerin inhibited in vivo growth of mouse melanoma and breast adenocarcinoma models. Growth inhibition was associated with an altered host response, and was abrogated by NK cell depletion. Intratumoral injection of chemerin also inhibited tumors, suggesting the potential for therapeutic application. We conclude that chemerin is an endogenous tumor suppressive chemoattractant cytokine whose downregulation in neoplasia contributes to immune evasion and tumor growth.

Clinical Trials

  • Clinical and Pathologic Studies of Patients Undergoing Treatment With EGFR Inhibitors Not Recruiting

    Cetuximab, erlotinib, and panitumumab are all recently FDA approved epidermal growth factor receptor (EGFR) inhibitors that treat a wide variety of tumor types, such as colon, lung, and head and neck. Blockade of the EGFR results in inhibition of multiple downstream pathways, leading to slowed tumor growth. In addition, these inhibitors may enhance anti-tumor immune responses through uncharacterized mechanisms. While producing significant responses in many settings, EGFR inhibitors also result in significant skin toxicity (rash) in a high percentage of patients. Multiple studies have correlated the presence and severity of rash with clinical response. Unfortunately, severe rash can often lead to dose delays, reductions, or even discontinuation of EGFR inhibitors, thus limiting their efficacy. The mechanism of both the rash and its correlation with tumor response is poorly understood. Skin biopsies display a robust leukocyte infiltrate, but a systematic analysis of the type of infiltrating leukocytes, activation state, or homing receptor expression has not been performed. Chemokines and chemokine receptors control leukocyte trafficking to the skin and other tissue sites, and defined receptor profiles for skin-, gut-, and lung-homing leukocytes are well established. In this study, the investigators propose to evaluate the homing phenotype of leukocytes from peripheral blood and skin biopsies of patients receiving EGFR inhibitors. The investigators will use RNA microarrays to evaluate the expression of chemokines and other key genes regulated in skin during treatment. The investigators will utilize in vitro methods to investigate effects of EGFR inhibitors on imprinting of T cell tissue-specific homing receptors. The investigators will examine correlations among the pathologic data, clinical findings, and tumor response. If validated, peripheral blood evaluation could potentially be used as a predictive indicator for patients receiving EGFR inhibitors. This study may also identify novel targets for limiting skin toxicity while receiving EGFR inhibitors, thus allowing maximal dosing and clinical response from these agents.

    Stanford is currently not accepting patients for this trial. For more information, please contact Russell Pachynski, (650) 906 - 6530.

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  • Provide Expanded Access to MDV3100 and Monitor Its Safety in Patients With Progressive Castration-Resistant Prostate Cancer Previously Treated With Docetaxel-Based Chemotherapy Not Recruiting

    The purpose of this treatment protocol is to provide expanded access to MDV3100 and monitor its safety in patients with metastatic castration-resistant prostate cancer previously treated with docetaxel-based chemotherapy.

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, (650) 736 - 1252.

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  • Sunitinib Malate With or Without Gemcitabine Hydrochloride in Treating Patients With Advanced Kidney Cancer That Cannot Be Removed By Surgery Recruiting

    RATIONALE: Sunitinib malate may stop the growth of tumor cells by blocking some of the enzymes needed for cell growth or by blocking blood flow to the tumor. Drugs used in chemotherapy, such as gemcitabine hydrochloride, work in different ways to stop the growth or tumor cells, either by killing the cells or by stopping them from dividing. It is not yet known whether giving sunitinib malate and gemcitabine hydrochloride together is more effective than sunitinib malate alone in treating patients with kidney cancer. PURPOSE: This randomized phase II clinical trial is studying giving sunitinib malate together with or without gemcitabine hydrochloride to see how well they work in treating patients with advanced kidney cancer that cannot be removed by surgery.

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  • A Safety and Efficacy Study of Oral MDV3100 in Chemotherapy-Naive Patients With Progressive Metastatic Prostate Cancer Not Recruiting

    The purpose of this study is to determine the benefit of MDV3100 versus placebo as assessed by overall survival and progression-free survival in patients with progressive metastatic prostate cancer who have failed androgen deprivation therapy but not yet received chemotherapy.

    Stanford is currently not accepting patients for this trial. For more information, please contact Sarah Barbeau, (650) 723 - 6286.

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  • BMS-936558 (MDX-1106) In Subjects With Advanced/Metastatic Clear-Cell Renal Cell Carcinoma (RCC) Not Recruiting

    The purpose of this study is to measure how active BMS-936558 is against Renal Cell Carcinoma (RCC) as measured by the disease not progressing and whether a dose response relationship exists.

    Stanford is currently not accepting patients for this trial. For more information, please contact Sarah Barbeau, (650) 723 - 6286.

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  • Temsirolimus to Reverse Androgen Insensitivity for Castration-resistant Prostate Cancer Not Recruiting

    There is a clear need for novel effective agents in castration-resistant prostate cancer (CRPC), an entity previously referred to as "androgen-insensitive" or "hormone-refractory" prostate cancer. While numerous therapies impact biochemical response in this disease, none improve overall survival outside of chemotherapy. The mechanisms behind progression to castration-resistance are unclear, but preclinical studies suggest that loss of the tumor suppressor gene PTEN and subsequent up-regulation of Akt, which is upstream of mTOR, may be involved in prostate cancer progression and metastasis. Based on these observations, we hypothesize that inhibition of mTOR activity with an IV mTOR inhibitor, temsirolimus, may prolong hormone sensitivity and delay disease progression. We have received approval and drug support from the NCCN and Wyeth to study temsirolimus in castration-resistant prostate cancer before antiandrogen withdrawal in a phase II, single stage, non-randomized clinical trial. Forty patients who are currently on combined androgen blockade with bicalutamide, who have evidence of disease progression by PSA or bony metastasis will receive temsirolimus weekly for 13 weeks. Because evaluating new therapies in prostate cancer is uniquely challenging given its long natural history and relatively indolent nature, this study will employ an established surrogate endpoint for efficacy, prostate-specific antigen (PSA), which will permit preliminary evaluation of this combination in fewer patients and in less time than would otherwise be possible in this disease, and additionally evaluates secondary time-to-event outcomes. By co-targeting the androgen and PTEN/Akt/mTOR signaling pathways in castration-resistant prostate cancer, we see great potential to impact this pervasive disease.

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, (650) 736 - 1252.

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  • DN24-02 as Adjuvant Therapy in Subjects With High Risk HER2+ Urothelial Carcinoma Not Recruiting

    This study is being conducted to examine survival, safety, and the magnitude of the immune response induced following administration of DN24-02 in subjects with HER2+ urothelial carcinoma.

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, (650) 736 - 1252.

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  • Study of Abiraterone Acetate in Patients With Advanced Prostate Cancer Not Recruiting

    The purpose of this study is to collect additional safety information on abiraterone acetate administered with prednisone to patients with metastatic castration-resistant prostate cancer (CRPC).

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, (650) 736 - 1252.

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  • Study of Itraconazole in Castration Resistant Prostate Cancer (CRPC) Post Docetaxel Chemotherapy Not Recruiting

    Assess the efficacy of itraconazole as an anticancer drug in CRPC as measured by a drop in serum PSA

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, (650) 736 - 1252.

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  • Radium-223 Dichloride (BAY88-8223) in Castration-Resistant (Hormone-Refractory) Prostate Cancer Patients With Bone Metastases Recruiting

    This study is a prospective, interventional, open-label, multi-center early access program for the use of Ra-223 Cl2 in HRPC/CRPC patients diagnosed with symptomatic bone metastasis and to collect additional short and long term safety data on the product.

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  • A Study to Evaluate Pazopanib as an Adjuvant Treatment for Localized Renal Cell Carcinoma (RCC) Not Recruiting

    This randomized Phase III study is to evaluate whether pazopanib compared with placebo can prevent or delay recurrence of kidney cancer in patients with moderately high or high risk of developing recurrence after undergoing kidney cancer surgery

    Stanford is currently not accepting patients for this trial. For more information, please contact Denise Haas, 650736-1252.

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  • Study of Dovitinib Versus Sorafenib in Patients With Metastatic Renal Cell Carcinoma Not Recruiting

    This study will evaluate the safety and efficacy of Dovitinib versus sorafenib in patients with metastatic renal cell cancer.

    Stanford is currently not accepting patients for this trial. For more information, please contact Sarah Barbeau, (650) 723 - 6286.

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Journal Articles

  • The chemoattractant chemerin suppresses melanoma by recruiting natural killer cell antitumor defenses JOURNAL OF EXPERIMENTAL MEDICINE Pachynski, R. K., Zabel, B. A., Kohrt, H. E., Tejeda, N. M., Monnier, J., Swanson, C. D., Holzer, A. K., Gentles, A. J., Sperinde, G. V., Edalati, A., Hadeiba, H. A., Alizadeh, A. A., Butcher, E. C. 2012; 209 (8): 1427-1435


    Infiltration of specialized immune cells regulates the growth and survival of neoplasia. Here, in a survey of public whole genome expression datasets we found that the gene for chemerin, a widely expressed endogenous chemoattractant protein, is down-regulated in melanoma as well as other human tumors. Moreover, high chemerin messenger RNA expression in tumors correlated with improved outcome in human melanoma. In experiments using the B16 transplantable mouse melanoma, tumor-expressed chemerin inhibited in vivo tumor growth without altering in vitro proliferation. Growth inhibition was associated with an altered profile of tumor-infiltrating cells with an increase in natural killer (NK) cells and a relative reduction in myeloid-derived suppressor cells and putative immune inhibitory plasmacytoid dendritic cells. Tumor inhibition required host expression of CMKLR1 (chemokine-like receptor 1), the chemoattractant receptor for chemerin, and was abrogated by NK cell depletion. Intratumoral injection of chemerin also inhibited tumor growth, suggesting the potential for therapeutic application. These results show that chemerin, whether expressed by tumor cells or within the tumor environment, can recruit host immune defenses that inhibit tumorigenesis and suggest that down-regulation of chemerin may be an important mechanism of tumor immune evasion.

    View details for DOI 10.1084/jem.20112124

    View details for Web of Science ID 000307016500006

    View details for PubMedID 22753924

  • Plasmacytoid Dendritic Cells Transport Peripheral Antigens to the Thymus to Promote Central Tolerance IMMUNITY Hadeiba, H., Lahl, K., Edalati, A., Oderup, C., Habtezion, A., Pachynski, R., Nguyen, L., Ghodsi, A., Adler, S., Butcher, E. C. 2012; 36 (3): 438-450


    Central tolerance can be mediated by peripheral dendritic cells (DCs) that transport innocuous antigens (Ags) to the thymus for presentation to developing T cells, but the responsible DC subsets remained poorly defined. Immature plasmacytoid DCs (pDCs) express CCR9, a chemokine receptor involved in migration of T cell precursors to the thymus. We show here that CCR9 mediated efficient thymic entry of endogenous or i.v. transfused pDCs. pDCs activated by Toll-like receptor (TLR) ligands downregulated CCR9 and lost their ability to home to the thymus. Moreover, endogenous pDCs took up subcutaneously injected fluorescent Ag and, in the absence of TLR signals, transported Ag to the thymus in a CCR9-dependent fashion. Injected, Ag-loaded pDCs effectively deleted Ag-specific thymocytes, and this thymic clonal deletion required CCR9-mediated homing and was prevented by infectious signals. Thus, peripheral pDCs can contribute to immune tolerance through CCR9-dependent transport of peripheral Ags and subsequent deletion of Ag-reactive thymocytes.

    View details for DOI 10.1016/j.immuni.2012.01.017

    View details for Web of Science ID 000302048400015

    View details for PubMedID 22444632

  • Extranodal dissemination of non-Hodgkin lymphoma requires CD47 and is inhibited by anti-CD47 antibody therapy BLOOD Chao, M. P., Tang, C., Pachynski, R. K., Chin, R., Majeti, R., Weissman, I. L. 2011; 118 (18): 4890-4901


    Non-Hodgkin lymphoma (NHL) presents as both localized and disseminated disease with spread to secondary sites carrying a worse prognosis. Although pathways driving NHL dissemination have been identified, there are few therapies capable of inhibiting them. Here, we report a novel role for the immunomodulatory protein CD47 in NHL dissemination, and we demonstrate that therapeutic targeting of CD47 can prevent such spread. We developed 2 in vivo lymphoma metastasis models using Raji cells, a human NHL cell line, and primary cells from a lymphoma patient. CD47 expression was required for Raji cell dissemination to the liver in mouse xenotransplants. Targeting of CD47 with a blocking antibody inhibited Raji cell dissemination to major organs, including the central nervous system, and inhibited hematogenous dissemination of primary lymphoma cells. We hypothesized that anti-CD47 antibody-mediated elimination of circulating tumor cells occurred through phagocytosis, a previously described mechanism for blocking anti-CD47 antibodies. As predicted, inhibition of dissemination by anti-CD47 antibodies was dependent on blockade of phagocyte SIRP? and required macrophage effector cells. These results demonstrate that CD47 is required for NHL dissemination, which can be therapeutically targeted with a blocking anti-CD47 antibody. Ultimately, these findings are potentially applicable to the dissemination and metastasis of other solid tumors.

    View details for DOI 10.1182/blood-2011-02-338020

    View details for Web of Science ID 000296714500018

    View details for PubMedID 21828138

  • CD137 stimulation enhances the antilymphoma activity of anti-CD20 antibodies BLOOD Kohrt, H. E., Houot, R., Goldstein, M. J., Weiskopf, K., Alizadeh, A. A., Brody, J., Mueller, A., Pachynski, R., Czerwinski, D., Coutre, S., Chao, M. P., Chen, L., Tedder, T. F., Levy, R. 2011; 117 (8): 2423-2432


    Antibody-dependent cell-mediated cytotoxicity (ADCC), which is largely mediated by natural killer (NK) cells, is thought to play an important role in the efficacy of rituximab, an anti-CD20 monoclonal antibody (mAb) used to treat patients with B-cell lymphomas. CD137 is a costimulatory molecule expressed on a variety of immune cells after activation, including NK cells. In the present study, we show that an anti-CD137 agonistic mAb enhances the antilymphoma activity of rituximab by enhancing ADCC. Human NK cells up-regulate CD137 after encountering rituximab-coated tumor B cells, and subsequent stimulation of these NK cells with anti-CD137 mAb enhances rituximab-dependent cytotoxicity against the lymphoma cells. In a syngeneic murine lymphoma model and in a xenotransplanted human lymphoma model, sequential administration of anti-CD20 mAb followed by anti-CD137 mAb had potent antilymphoma activity in vivo. These results support a novel, sequential antibody approach against B-cell malignancies by targeting first the tumor and then the host immune system.

    View details for DOI 10.1182/blood-2010-08-301945

    View details for Web of Science ID 000287698800023

    View details for PubMedID 21193697

  • Prostate specific antigen doubling time (PSADT) in patients with hormone refractory prostate cancer (HRPC) undergoing docetaxel chemotherapy as a predictor of overall survival. Journal of Clinical Oncology, 2007 ASCO Annual Meeting Proceedings Pachynski RK, King C, Srinivas S 2007; 25 (18s): 15556
  • Redirecting migration of T cells to chemokine secreted from tumors by genetic modification with CXCR2 HUMAN GENE THERAPY Kershaw, M. H., Wang, G., Westwood, J. A., Pachynski, R. K., Tiffany, H. L., Marincola, F. M., Wang, E., Young, H. A., Murphy, P. M., Hwu, P. 2002; 13 (16): 1971-1980


    T-cell-based immunotherapies provide a promising means of cancer treatment although durable antitumor responses are infrequent. A potential reason for these shortcomings may lie in the observed lack of trafficking of specific T cells to tumor. Our increasing knowledge of the process of trafficking involving adhesion molecules and chemokines affords us the opportunity to intervene and correct deficiencies in this process. Chemokines can be expressed by a range of tumors and may serve as suitable targets for directing specific T cells toward tumor. We initially sought to identify which chemokines were produced by a range of human tumor cell lines, and which chemokines and chemokine receptors were expressed by cultured T cells. We identified two chemokines: Growth-Regulated Oncogene-alpha (Gro-alpha; CXCL1) and Regulated on Activation Normal T Cell-Expressed and Secreted (RANTES; CCL5), to be secreted by several human tumor cell lines. Expression was also detected in fine-needle aspirates of melanoma from patients. In addition, we determined the expression of several chemokine receptors on cultured human T cells including CCR1, CCR2, CCR4, CCR5, CXCR3, and CXCR4. Cultured, activated human T cells expressed the chemokines lymphotactin (XCL1), RANTES, macrophage inflammatory protein-1 alpha (MIP-1 alpha; CCL3) and MIP-1 beta (CCL4), but no appreciable Gro-alpha. In a strategy to direct T cells toward chemokines expressed by tumors we chose Gro-alpha as the target chemokine because it was produced by tumor and not by T cells themselves. However, T cells did not express the receptor for Gro-alpha, CXCR2, and therefore, T cells were transduced with a retroviral vector encoding CXCR2. Calcium ion mobilization, an important first step in chemokine receptor signaling, was subsequently demonstrated in transduced T cells in response to Gro-alpha. In addition, Gro-alpha was chemotactic for T cells expressing CXCR2 in vitro toward both recombinant protein and tumor-derived chemokine. Interestingly we demonstrate, for the first time, that Gro-alpha was able to induce interferon-gamma (IFN-gamma) secretion from transduced T cells, thereby extending our knowledge of other potential functions of CXCR2. This study demonstrates the feasibility of redirecting the migration properties of T cells toward chemokines secreted by tumors.

    View details for Web of Science ID 000188327800005

    View details for PubMedID 12427307

  • Secondary lymphoid-tissue chemokine (SLC) stimulates integrin alpha(4)beta(7)-mediated adhesion of lymphocytes to mucosal addressin cell adhesion molecule-1 (MAdCAM-1) under flow JOURNAL OF IMMUNOLOGY Pachynski, R. K., Wu, S. W., Gunn, M. D., Erle, D. J. 1998; 161 (2): 952-956


    The attachment of leukocytes to the endothelium is a multistep process that depends upon a very rapid increase in the adhesive activity of leukocyte integrins. A pertussis toxin-sensitive pathway stimulates integrin-dependent lymphocyte adhesion to Peyer's patch high endothelial venules in vivo, but the factors responsible for activating this pathway have not been identified previously. We now report that secondary lymphoid-tissue chemokine (SLC) (also known as 6Ckine, Exodus-2, and thymus-derived chemotactic agent 4), a recently described CC chemokine that is expressed in Peyer's patches and lymph nodes, rapidly activates integrin-mediated lymphocyte adhesion. Immobilized SLC increased the adhesion of HUT-78 T cells and human PBLs to mucosal addressin cell adhesion molecule-1, a protein that is expressed on Peyer's patch and mesenteric lymph node high endothelial venules. This effect of SLC was seen in both static and flow chamber adhesion assays, was mediated by integrin alpha 4 beta 7, and was inhibited by pertussis toxin. The other CC chemokines tested did not increase adhesion to mucosal addressin cell adhesion molecule-1. SLC had a greater effect on naive CD4+ T cells than on memory CD4+ T cells; CD8+ T cells, B cells, and NK cells were also responsive to SLC. SLC is likely to play an important role in regulating the recruitment of lymphocytes to Peyer's patches and lymph nodes.

    View details for Web of Science ID 000074728400051

    View details for PubMedID 9670974

  • Presentation of integrins on leukocyte microvilli: A role for the extracellular domain in determining membrane localization JOURNAL OF CELL BIOLOGY Abitorabi, M. A., Pachynski, R. K., Ferrando, R. E., Tidswell, M., Erle, D. J. 1997; 139 (2): 563-571


    Adhesion of blood leukocytes to the endothelium involves multiple steps including initial attachment (tethering), rolling, and firm arrest. Presentation of adhesion molecules on leukocyte microvilli can substantially enhance tethering. Localization of L-selectin to microvilli and of CD44 to the planar cell body have been shown to depend upon their transmembrane and cytoplasmic domains. We investigated the role of leukocyte integrin transmembrane and cytoplasmic domains in initiating adhesion under flow and in microvillous localization. Integrins alpha4beta7, alphaLbeta2, and alphaMbeta2 were heterologously expressed in K562 cells. alpha4beta7 initiated adhesion under flow and localized to microvilli, whereas beta2 integrins did not initiate adhesion and localized to the cell body. Chimeric integrins were produced by replacing the alpha4beta7 cytoplasmic and/or transmembrane domains with the homologous domains of alphaLbeta2 or alphaMbeta2. Unexpectedly, these chimeras efficiently mediated adhesion to the alpha4beta7 ligand mucosal addressin cell adhesion molecule-1 under flow and localized to microvilli. Therefore, differences between the transmembrane and cytoplasmic domains of alpha4 and beta2 integrins do not account for differences in ability to support attachment under flow or in membrane localization. Integrins alpha4beta1, alpha5beta1, alpha6Abeta1, alphavbeta3, and alphaEbeta7 also localized to microvilli. Transmembrane proteins known or suspected to associate with extracellular domains of microvillous integrins, including tetraspans and CD47, were concentrated on microvilli as well. These findings suggest that interactions between the extracellular domains of integrins and associated proteins could direct the assembly of multimolecular complexes on leukocyte microvilli.

    View details for Web of Science ID A1997YC38600022

    View details for PubMedID 9334357

  • Structure-function analysis of the integrin beta(7) subunit - Identification of domains involved in adhesion to MAdCAM-1 JOURNAL OF IMMUNOLOGY Tidswell, M., Pachynski, R., Wu, S. W., Qiu, S. Q., Dunham, E., Cochran, N., Briskin, M. J., Kilshaw, P. J., Lazarovits, A. I., Andrew, D. P., BUTCHER, E. C., YEDNOCK, T. A., Erle, D. J. 1997; 159 (3): 1497-1505


    Beta 7 integrins serve special roles in mucosal immunity. Alpha 4 beta 7-mediated adhesion to mucosal addressin cell adhesion molecule-1 (MAdCAM-1) directs lymphocyte homing to the gut, and alpha E beta 7 mediates binding of lymphocytes to E-cadherin on epithelial cells. Since alpha 4 beta 7 mediates adhesion to MAdCAM-1 but alpha 4 beta 1 does not, we used beta 7/beta 1 chimeras to directly assess the importance of specific regions of beta 7 in MAdCAM-1 binding. We found a region of beta 7 (residues 46-386) that accounts for specificity of alpha 4 beta 7 binding to MAdCAM-1. We also used human/mouse and human/rat chimeric beta 7 subunits to map epitopes recognized by fifteen anti-beta 7 mAbs. Six of seven Abs that block adhesion to MAdCAM-1 and E-cadherin (Fib 21, 22, 27, 30, 504; Act-1) mapped to amino acid residues 176-250. Residues 176-250 lie within the region of beta 7 that specifies MAdCAM-1 binding and also within a region that has a predicted structure homologous to the metal ion-dependent adhesion site (MIDAS) domains of the integrin subunits alpha L and alpha M. Three new Abs that recognize beta 7 in the presence of Mn2+, but not Ca2+, and promote adhesion to MAdCAM-1, mapped to amino acids 46-149. One blocking and five other Abs mapped to other regions (amino acids 387-725). We conclude that a MIDAS-like domain serves a critical role in beta 7 integrin-mediated adhesion.

    View details for Web of Science ID A1997XL78900055

    View details for PubMedID 9233649

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