PMID- 10652291
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - Collagen XVII is destabilized by a glycine substitution mutation in the cell
      adhesion domain Col15.
PG  - 3093-9
AB  - Collagen XVII is a hemidesmosomal transmembrane molecule important for epithelial
      adhesion in the skin. It exists in two forms, as a full-length protein and as a
      soluble ectodomain that is shed from the keratinocyte surface by furin-mediated
      proteolysis. To obtain information on the conformation and the functions of this 
      unusual collagen, its largest collagenous domain, Col15, was expressed in a
      eukaryotic episomal expression system and purified by DEAE and fast protein
      liquid- Mono S chromatography. The protein was triple-helical (T(m) of 26.5
      degrees C) when produced in cultures containing ascorbic acid. When the vitamin
      supply was limited, the 4-hydroxyproline content was reduced from 74 to 9%,
      which, in turn, resulted in a drastic reduction of the stability of the triple
      helix. The glycine substitution mutation G627V associated with junctional
      epidermolysis bullosa, a human blistering skin disease, also had a striking
      effect on thermal stability of rCol15 causing partial unfolding already at 4
      degrees C. Col15 promoted cell adhesion of epithelial and fibroblastic cell lines
      with a beta1 integrin-mediated mechanism. In concert with this, in acquired
      autoimmune blistering skin diseases, circulating IgG and IgA autoantibodies were 
      found to target rCol15r.
FAU - Tasanen, K
AU  - Tasanen K
AD  - Department of Dermatology, University of Munster, 48149 Munster, Germany.
FAU - Eble, J A
AU  - Eble JA
FAU - Aumailley, M
AU  - Aumailley M
FAU - Schumann, H
AU  - Schumann H
FAU - Baetge, J
AU  - Baetge J
FAU - Tu, H
AU  - Tu H
FAU - Bruckner, P
AU  - Bruckner P
FAU - Bruckner-Tuderman, L
AU  - Bruckner-Tuderman L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Autoantigens)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DST protein, human)
RN  - 0 (Dystonin)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Non-Fibrillar Collagens)
RN  - 0 (collagen type XVII)
RN  - 9007-34-5 (Collagen)
RN  - TE7660XO1C (Glycine)
SB  - IM
MH  - Amino Acid Substitution
MH  - Autoantigens/*chemistry/*genetics
MH  - *Carrier Proteins
MH  - Cell Adhesion
MH  - Circular Dichroism
MH  - Collagen/*chemistry/*genetics
MH  - *Cytoskeletal Proteins
MH  - Dystonin
MH  - Glycine/chemistry/genetics
MH  - Humans
MH  - *Nerve Tissue Proteins
MH  - *Non-Fibrillar Collagens
MH  - Point Mutation
MH  - Protein Conformation
MH  - Structure-Activity Relationship
EDAT- 2000/02/01 09:00
MHDA- 2000/03/18 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/03/18 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3093 [doi]
AID - S0021-9258(18)30880-9 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3093-9. doi: 10.1074/jbc.275.5.3093.