Transglutaminase cross-linking properties of the small proline-rich 1 family of cornified cell envelope proteins: Integration with loricrin

Eleonora Candi, Edit Tarcsa, William W. Idler, Tonja Kartasova, Lyuben N. Marekov, Peter M. Steinert

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

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 α or β 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.

Original languageEnglish
Pages (from-to)7226-7237
Number of pages12
JournalJournal of Biological Chemistry
Volume274
Issue number11
DOIs
Publication statusPublished - Mar 12 1999

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Transglutaminases
Proline
Proteins
Enzymes
Epithelium
Head
Oligomerization
Dichroism
Circular Dichroism
loricrin
Keratinocytes
Oligomers
Crosslinking
transglutaminase 1
Bacteria
Polymers
Databases
Peptides
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Transglutaminase cross-linking properties of the small proline-rich 1 family of cornified cell envelope proteins : Integration with loricrin. / Candi, Eleonora; Tarcsa, Edit; Idler, William W.; Kartasova, Tonja; Marekov, Lyuben N.; Steinert, Peter M.

In: Journal of Biological Chemistry, Vol. 274, No. 11, 12.03.1999, p. 7226-7237.

Research output: Contribution to journalArticle

Candi, Eleonora ; Tarcsa, Edit ; Idler, William W. ; Kartasova, Tonja ; Marekov, Lyuben N. ; Steinert, Peter M. / Transglutaminase cross-linking properties of the small proline-rich 1 family of cornified cell envelope proteins : Integration with loricrin. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 11. pp. 7226-7237.
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