Proteolytic release of keratinocyte transglutaminase

R. H. Rice, X. Rong, R. Chakravarty

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Human keratinocytes express a particulate transglutaminase that can be released from the membranes by limited proteolysis with trypsin or plasmin to yield a form that is ≃ 80 kDa. The enzyme from cultured cells was also releasable by endogenous proteolysis to yield a catalytically active fragment of ≃ 80 kDa. Endogenous release was strongly dependent upon temperature and Ca2+ concentration and was inhibited by iodoacetate, but not by leupeptin, antipain or phenylmethanesulphonyl fluoride. These phenomena raise the possibility of partial translocation of transglutaminase activity to the cytoplasm by proteolysis to which the enzyme is subject during terminal differentiation. In addition, hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution (79 kDa), whereas that solubilized by hydroxylamine without proteolysis appeared dimeric (190 kDa). The latter dimeric state may reflect either an altered conformation of the enzyme or post-translational modification beyond fatty acid esterification.

Original languageEnglish (US)
Pages (from-to)351-357
Number of pages7
JournalBiochemical Journal
Volume265
Issue number2
StatePublished - 1990

Fingerprint

Proteolysis
Transglutaminases
Keratinocytes
Enzymes
Antipain
Iodoacetates
Hydroxylamine
Esterification
Fibrinolysin
Hydrodynamics
Post Translational Protein Processing
Fluorides
Trypsin
Conformations
Cultured Cells
Cytoplasm
Fatty Acids
Cells
Membranes
Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Rice, R. H., Rong, X., & Chakravarty, R. (1990). Proteolytic release of keratinocyte transglutaminase. Biochemical Journal, 265(2), 351-357.

Proteolytic release of keratinocyte transglutaminase. / Rice, R. H.; Rong, X.; Chakravarty, R.

In: Biochemical Journal, Vol. 265, No. 2, 1990, p. 351-357.

Research output: Contribution to journalArticle

Rice, RH, Rong, X & Chakravarty, R 1990, 'Proteolytic release of keratinocyte transglutaminase', Biochemical Journal, vol. 265, no. 2, pp. 351-357.
Rice RH, Rong X, Chakravarty R. Proteolytic release of keratinocyte transglutaminase. Biochemical Journal. 1990;265(2):351-357.
Rice, R. H. ; Rong, X. ; Chakravarty, R. / Proteolytic release of keratinocyte transglutaminase. In: Biochemical Journal. 1990 ; Vol. 265, No. 2. pp. 351-357.
@article{addf5fafa5284921ac0c5f573f5e39a0,
title = "Proteolytic release of keratinocyte transglutaminase",
abstract = "Human keratinocytes express a particulate transglutaminase that can be released from the membranes by limited proteolysis with trypsin or plasmin to yield a form that is ≃ 80 kDa. The enzyme from cultured cells was also releasable by endogenous proteolysis to yield a catalytically active fragment of ≃ 80 kDa. Endogenous release was strongly dependent upon temperature and Ca2+ concentration and was inhibited by iodoacetate, but not by leupeptin, antipain or phenylmethanesulphonyl fluoride. These phenomena raise the possibility of partial translocation of transglutaminase activity to the cytoplasm by proteolysis to which the enzyme is subject during terminal differentiation. In addition, hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution (79 kDa), whereas that solubilized by hydroxylamine without proteolysis appeared dimeric (190 kDa). The latter dimeric state may reflect either an altered conformation of the enzyme or post-translational modification beyond fatty acid esterification.",
author = "Rice, {R. H.} and X. Rong and R. Chakravarty",
year = "1990",
language = "English (US)",
volume = "265",
pages = "351--357",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",

}

TY - JOUR

T1 - Proteolytic release of keratinocyte transglutaminase

AU - Rice, R. H.

AU - Rong, X.

AU - Chakravarty, R.

PY - 1990

Y1 - 1990

N2 - Human keratinocytes express a particulate transglutaminase that can be released from the membranes by limited proteolysis with trypsin or plasmin to yield a form that is ≃ 80 kDa. The enzyme from cultured cells was also releasable by endogenous proteolysis to yield a catalytically active fragment of ≃ 80 kDa. Endogenous release was strongly dependent upon temperature and Ca2+ concentration and was inhibited by iodoacetate, but not by leupeptin, antipain or phenylmethanesulphonyl fluoride. These phenomena raise the possibility of partial translocation of transglutaminase activity to the cytoplasm by proteolysis to which the enzyme is subject during terminal differentiation. In addition, hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution (79 kDa), whereas that solubilized by hydroxylamine without proteolysis appeared dimeric (190 kDa). The latter dimeric state may reflect either an altered conformation of the enzyme or post-translational modification beyond fatty acid esterification.

AB - Human keratinocytes express a particulate transglutaminase that can be released from the membranes by limited proteolysis with trypsin or plasmin to yield a form that is ≃ 80 kDa. The enzyme from cultured cells was also releasable by endogenous proteolysis to yield a catalytically active fragment of ≃ 80 kDa. Endogenous release was strongly dependent upon temperature and Ca2+ concentration and was inhibited by iodoacetate, but not by leupeptin, antipain or phenylmethanesulphonyl fluoride. These phenomena raise the possibility of partial translocation of transglutaminase activity to the cytoplasm by proteolysis to which the enzyme is subject during terminal differentiation. In addition, hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution (79 kDa), whereas that solubilized by hydroxylamine without proteolysis appeared dimeric (190 kDa). The latter dimeric state may reflect either an altered conformation of the enzyme or post-translational modification beyond fatty acid esterification.

UR - http://www.scopus.com/inward/record.url?scp=0025022625&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025022625&partnerID=8YFLogxK

M3 - Article

C2 - 1967934

AN - SCOPUS:0025022625

VL - 265

SP - 351

EP - 357

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -