Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Research Project (R01)
Project #
3R01DE008648-05S1
Application #
3222447
Study Section
Oral Biology and Medicine Subcommittee 1 (OBM)
Project Start
1988-09-01
Project End
1994-08-31
Budget Start
1992-09-01
Budget End
1993-08-31
Support Year
5
Fiscal Year
1993
Total Cost
Indirect Cost
Name
University of Maryland Baltimore
Department
Type
Schools of Dentistry
DUNS #
003255213
City
Baltimore
State
MD
Country
United States
Zip Code
21201
Hebert, C; Norris, K; Della Coletta, R et al. (1999) Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. J Cell Biochem 73:248-58
Coletta, R D; Almeida, O P; Ferreira, L R et al. (1999) Increase in expression of Hsp47 and collagen in hereditary gingival fibromatosis is modulated by stress and terminal procollagen N-propeptides. Connect Tissue Res 40:237-49
Coletta, R D; Almeida, O P; Reynolds, M A et al. (1999) Alteration in expression of MMP-1 and MMP-2 but not TIMP-1 and TIMP-2 in hereditary gingival fibromatosis is mediated by TGF-beta 1 autocrine stimulation. J Periodontal Res 34:457-63
Sauk, J J; Norris, K; Hebert, C et al. (1998) Hsp47 binds to the KDEL receptor and cell surface expression is modulated by cytoplasmic and endosomal pH. Connect Tissue Res 37:105-19
Ferreira, L R; Norris, K; Smith, T et al. (1996) Hsp47 and other ER-resident molecular chaperones form heterocomplexes with each other and with collagen type IV chains. Connect Tissue Res 33:265-73
D'Errico, J A; Sauk, J J; Prince, C W et al. (1995) Osteopontin adhesion receptors on gingival fibroblasts. J Periodontal Res 30:34-41
Smith, T; Ferreira, L R; Hebert, C et al. (1995) Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J Biol Chem 270:18323-8
Hu, G; Gura, T; Sabsay, B et al. (1995) Endoplasmic reticulum protein Hsp47 binds specifically to the N-terminal globular domain of the amino-propeptide of the procollagen I alpha 1 (I)-chain. J Cell Biochem 59:350-67
Sun, D; Sauk, J J; Archibald, D W (1994) Decrease of heat shock protein 27/28 with heat stress in HTLV-I-transformed cells. Exp Mol Pathol 60:147-57
Ferreira, L R; Norris, K; Smith, T et al. (1994) Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones. J Cell Biochem 56:518-26

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