PMID- 10066784
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 11
DP  - 1999 Mar 12
TI  - Transglutaminase cross-linking properties of the small proline-rich 1 family of
      cornified cell envelope proteins. Integration with loricrin.
PG  - 7226-37
AB  - Small proline-rich 1 (SPR1) proteins are important for barrier function in
      stratified squamous epithelia. To explore their properties, we expressed in
      bacteria a recombinant human SPR1 protein and isolated native SPR1 proteins from 
      cultured mouse keratinocytes. By circular dichroism, they possess no alpha or
      beta structure but have some organized structure associated with their central
      peptide repeat domain. The transglutaminase (TGase) 1 and 3 enzymes use the SPR1 
      proteins as complete substrates in vitro but in different ways: head domain A
      sequences at the amino terminus were used preferentially for cross-linking by
      TGase 3, whereas those in head domain B sequences were used for cross-linking by 
      TGase 1. The TGase 2 enzyme cross-linked SPR1 proteins poorly. Together with our 
      data base of 141 examples of in vivo cross-links between SPRs and loricrin, this 
      means that both TGase 1 and 3 are required for cross-linking SPR1 proteins in
      epithelia in vivo. Double in vitro cross-linking experiments suggest that
      oligomerization of SPR1 into large polymers can occur only by further TGase 1
      cross-linking of an initial TGase 3 reaction. Accordingly, we propose that TGase 
      3 first cross-links loricrin and SPRs together to form small interchain
      oligomers, which are then permanently affixed to the developing CE by further
      cross-linking by the TGase 1 enzyme. This is consistent with the known
      consequences of diminished barrier function in TGase 1 deficiency models.
FAU - Candi, E
AU  - Candi E
AD  - Laboratory of Skin Biology, NIAMS, National Institutes of Health, Bethesda,
      Maryland 20892-2752, USA.
FAU - Tarcsa, E
AU  - Tarcsa E
FAU - Idler, W W
AU  - Idler WW
FAU - Kartasova, T
AU  - Kartasova T
FAU - Marekov, L N
AU  - Marekov LN
FAU - Steinert, P M
AU  - Steinert PM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Membrane Proteins)
RN  - 0 (Peptides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (loricrin)
RN  - EC 2.3.2.13 (Transglutaminases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Membrane/metabolism
MH  - Cells, Cultured
MH  - Cloning, Molecular
MH  - Cross-Linking Reagents/metabolism
MH  - Humans
MH  - Keratinocytes/metabolism
MH  - Kinetics
MH  - Membrane Proteins/genetics/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Peptides/genetics/*metabolism
MH  - Proline-Rich Protein Domains
MH  - Recombinant Proteins/genetics/metabolism
MH  - Transglutaminases/*metabolism
EDAT- 1999/03/06 00:00
MHDA- 1999/03/06 00:01
CRDT- 1999/03/06 00:00
PHST- 1999/03/06 00:00 [pubmed]
PHST- 1999/03/06 00:01 [medline]
PHST- 1999/03/06 00:00 [entrez]
AID - 10.1074/jbc.274.11.7226 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 12;274(11):7226-37. doi: 10.1074/jbc.274.11.7226.