Protein disulfide isomerase (PDI) catalyzes protein folding and thiol-disulfide interchange reactions. The enzyme is localized in the lumen of endoplasmic reticulum (ER) and is abundant in secretory cells of various tissues. In this study we describe the isolation and characterization from human pancreas of a new protein, PDIp, that is structurally and functionally related to PDIs. PDIp cDNA is 1,659 bp in length and predicts a protein with an open reading frame of 511 amino acids. PDIp amino acid sequence shows 46% identity and 66% similarity to that of human PDI. PDIp possesses two thioredoxin-like active sites (WCGHCQ and WCTHCK) and an endoplasmic reticulum retention signal sequence, KEEL, at the carboxyl terminus. Northern analysis of normal human tissues and various human tumor cell lines revealed PDIp mRNA (2.0 kb) expression only in the normal pancreas. Recombinant PDIp protein catalyzed reductive cleavage of insulin and renaturation of reduced RNaseA. Somatic cell genetics and fluorescence in situ hybridization localized the PDIp gene to the short arm of human chromosome 16. It is concluded that PDIp is a new member of the PDI family and is highly expressed in human pancreas.

Desilva, M., Lu, J., Donadel, G., Modi, W., Xie, H., Notkins, A., et al. (1996). Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA AND CELL BIOLOGY, 15(1), 9-16 [10.1089/dna.1996.15.9].

Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas

DONADEL, GIULIA;
1996-01

Abstract

Protein disulfide isomerase (PDI) catalyzes protein folding and thiol-disulfide interchange reactions. The enzyme is localized in the lumen of endoplasmic reticulum (ER) and is abundant in secretory cells of various tissues. In this study we describe the isolation and characterization from human pancreas of a new protein, PDIp, that is structurally and functionally related to PDIs. PDIp cDNA is 1,659 bp in length and predicts a protein with an open reading frame of 511 amino acids. PDIp amino acid sequence shows 46% identity and 66% similarity to that of human PDI. PDIp possesses two thioredoxin-like active sites (WCGHCQ and WCTHCK) and an endoplasmic reticulum retention signal sequence, KEEL, at the carboxyl terminus. Northern analysis of normal human tissues and various human tumor cell lines revealed PDIp mRNA (2.0 kb) expression only in the normal pancreas. Recombinant PDIp protein catalyzed reductive cleavage of insulin and renaturation of reduced RNaseA. Somatic cell genetics and fluorescence in situ hybridization localized the PDIp gene to the short arm of human chromosome 16. It is concluded that PDIp is a new member of the PDI family and is highly expressed in human pancreas.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore MED/04 - Patologia Generale
English
Con Impact Factor ISI
Phylogeny; Chromosomes, Human, Pair 16; Protein Disulfide-Isomerases; Humans; Pancreas; Amino Acid Sequence; Isomerases; Chromosome Mapping; Cloning, Molecular; Base Sequence; Sequence Alignment; Sequence Analysis; Molecular Sequence Data
Desilva, M., Lu, J., Donadel, G., Modi, W., Xie, H., Notkins, A., et al. (1996). Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA AND CELL BIOLOGY, 15(1), 9-16 [10.1089/dna.1996.15.9].
Desilva, M; Lu, J; Donadel, G; Modi, W; Xie, H; Notkins, A; Lan, M
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/53222
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