Serine Proteinases From Mast Cells and Skin

Schechter, Norman M.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
• Type: Research Project (R01)
• Project #: 5R01AR042931-03
• Application #: 2082483
• Study Section: Arthritis and Musculoskeletal and Skin Diseases Special Grants Review Committee (AMS)
• Project Start: 1993-12-27
• Project End: 1997-11-30
• Budget Start: 1995-12-01
• Budget End: 1996-11-30
• Support Year: 3
• Fiscal Year: 1996

Institution

• Name: University of Pennsylvania
• Department: Dermatology
• Type: Schools of Medicine
• DUNS #: 042250712
• City: Philadelphia
• State: PA
• Country: United States
• Zip Code: 19104

Publications

Lazaar, Aili L; Plotnick, Michael I; Kucich, Umberto et al. (2002) Mast cell chymase modifies cell-matrix interactions and inhibits mitogen-induced proliferation of human airway smooth muscle cells. J Immunol 169:1014-20

Plotnick, Michael I; Samakur, Madhurika; Wang, Zhi Mei et al. (2002) Heterogeneity in serpin-protease complexes as demonstrated by differences in the mechanism of complex breakdown. Biochemistry 41:334-42

Solivan, Suzanne; Selwood, Trevor; Wang, Zhe Mei et al. (2002) Evidence for diversity of substrate specificity among members of the chymase family of serine proteases. FEBS Lett 512:133-8

Cooley, J; Takayama, T K; Shapiro, S D et al. (2001) The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites. Biochemistry 40:15762-70

Estebanez-Perpina, E; Fuentes-Prior, P; Belorgey, D et al. (2000) Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue. Biol Chem 381:1203-14

Groutas, W C; Schechter, N M; He, S et al. (1999) Human chymase inhibitors based on the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold. Bioorg Med Chem Lett 9:2199-204

Pereira, P J; Wang, Z M; Rubin, H et al. (1999) The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity. J Mol Biol 286:163-73

Selwood, T; McCaslin, D R; Schechter, N M (1998) Spontaneous inactivation of human tryptase involves conformational changes consistent with conversion of the active site to a zymogen-like structure. Biochemistry 37:13174-83

Wang, Z; Walter, M; Selwood, T et al. (1998) Recombinant expression of human mast cell proteases chymase and tryptase. Biol Chem 379:167-74

Schechter, N M; Brass, L F; Lavker, R M et al. (1998) Reaction of mast cell proteases tryptase and chymase with protease activated receptors (PARs) on keratinocytes and fibroblasts. J Cell Physiol 176:365-73