Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We screened monoclonal antibodies to cell-surface proteins and selected an antibody, called 6H1, that recognizes a putative integrin-associated protein. The 6H1 monoclonal antibody (mAb) indirectly coprecipitated alpha 3 beta 1 and/or alpha 6 beta 1, but not alpha 2 beta 1, or alpha 5 beta 1 from Brij 96 detergent lysates of multiple cell lines. Large scale purification using the 6H1 mAb yielded a single protein of 45-60 kDa with an amino-terminal sequence that exactly matched CD63. Confirming that the 6H1 mAb recognized the CD63 protein, 6H1 and a known anti-CD63 mAb yielded identical coprecipitation results and identical colocalization into lysosomal granules containing cathepsin D. Furthermore, we used an established anti-CD63 mAb to detect this protein in an alpha 3 beta 1 immunoprecipitate, and also we observed VLA-3 and CD63 colocalization in cellular "footprints." Notably, the cytoplasmic domain of alpha 3 was neither required nor sufficient for CD63 association, suggesting that it occurred elsewhere within the alpha 3 beta 1 complex. Knowledge of these specific CD63-alpha 3 beta 1 and CD63-alpha 6 beta 1 biochemical associations should lead to critical insights into the specialized functions of alpha 3 beta 1, alpha 6 beta 1, and CD63.
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PMID:Specific association of CD63 with the VLA-3 and VLA-6 integrins. 762 79

VLA, expression was immunohistochemically investigated in 145 breast carcinomas. Frozen tissue sections were probed with monoclonal anti-VLA, using automated (Ventana ES 320 system) and quantitative (SAMBA 2005 image processor) immunoperoxidase. A positive anti-VLA, immunoreaction was observed in 86 tumors (23.5%) within epithelial cells of carcinomas. The positive surface in tumors varied from 3% to 38% (mean = 13.8%, SD=11.5) and was independent of the tumor size, grade, type and aneuploidy, and of nodal status. VLA(2) was significantly correlated with VCAM (p<0.01), VLA(2) (p<0.01), E cadherin (p=0.025), and CD44 v (p<0.01), and an inverse relationship was observed with Ki67/MIB 1 (p=0.0024) and P-53 (p=0.034). In contrast VLA, expression proved to be independent of Bcl-2, c-erbB-2, cathepsin D, tenascin, CD31, ELAM, RE, RP, PS2 immunohistochemical expression. The results suggest that VLA, expression in tumors is related to the regulation of other adhesion molecules involved in the metastasis process, but the prognostic significance and clinical relevance of VLA, immunodetection in breast carcinomas remain to be demonstrated.
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PMID:VLA(3)/integrin expression in breast carcinomas evaluated by automated and quantitative immunohistochemistry. 2152 84