Rat peritoneal mast cell carboxypeptidase: localization, purification, and enzymatic properties

Everitt, Michael T.; Neurath, Hans

doi:10.1016/0014-5793(80)80095-0

Cited by 74 publications

(42 citation statements)

References 21 publications

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“…2), and is a single polypeptide chain of 34,500 D by SDS-PAGE (Fig. 3) (6,9). It is active at neutral to alkaline pH, and is inhibited by PCI (9).…”

Section: Discussionmentioning

confidence: 99%

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Human mast cell carboxypeptidase. Purification and characterization.

Goldstein¹,

Kaempfer²,

Kealey³

et al. 1989

J. Clin. Invest.

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“…2), and is a single polypeptide chain of 34,500 D by SDS-PAGE (Fig. 3) (6,9). It is active at neutral to alkaline pH, and is inhibited by PCI (9).…”

Section: Discussionmentioning

confidence: 99%

“…A carboxypeptidase (CP)l activity, thought to be carboxypeptidase A (CPA) or CPA-like, has been identified in rodent mast cells (6,7) and purified from rat Address reprint requests to Dr. Goldstein peritoneal mast cells (6) and rat skeletal muscle (8). A CP activity was recently identified in highly purified human mast cells from lung (9).…”

Section: Introductionmentioning

confidence: 99%

Human mast cell carboxypeptidase. Purification and characterization.

Goldstein¹,

Kaempfer²,

Kealey³

et al. 1989

J. Clin. Invest.

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“…Numbers on the branches represent the least number of nucleotide substitutions that could give rise to the amino acid sequences at the tips. There are four groups of orthologues ( [1][2][3], [4,5], [6,7], and [8] To establish the molecular ancestry of MC-CPA within the carboxypeptidase gene family, an evolutionary tree was constructed for the 10 mature carboxypeptidase amino acid sequences, using the Fitch algorithm for generation of minimal nucleotide replacement trees from amino acid sequence data (53). The most parsimonious nucleotide replacement tree that could give rise to the different amino acid sequences is shown in Fig.…”

Section: Methodsmentioning

confidence: 99%

“…The number of nucleotide substitutions required to give the amino acid sequences are shown, and are depicted as the lengths of the branches. There are four groups of orthologues ( [1][2][3], [4,5], [6,7], and [8]), representing four modern mammalian carboxypeptidase genes and their species homologues. These groups are paralogous to each other, arising from three gene duplications at A, B, and I.…”

Section: Methodsmentioning

confidence: 99%

“…The mast cell carboxypeptidase A (MC-CPA)' enzymes of the rat, mouse, and human are homologous secretory granule metalloexopeptidases that have pH optima in the neutral to basic Address correspondence to Dr. Dale S. Reynolds range (1)(2)(3). The MC-CPAs resemble bovine pancreatic carboxypeptidase A (CPA) in cleaving COOH-terminal aromatic and aliphatic amino acid residues, although human MC-CPA differs from bovine CPA by failing to cleave des-Arg bradykinin and substance P (4).…”

Section: Introductionmentioning

confidence: 99%

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Cloning and characterization of the novel gene for mast cell carboxypeptidase A.

Reynolds

Gurley²,

Austen³

1992

J. Clin. Invest.

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Metallocarboxypeptidases

Vendrell¹,

Avilés²,

Fricker³

2004

Handbook of Metalloproteins

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Metallocarboxypeptidases (CP) catalyze the removal of C‐terminal amino acids from proteins and/or peptides. The different members of the CP family differ in their specificity for C‐terminal residues and physiological function and can be divided into two subfamilies. Members of the A/B subfamily are generally produced as proenzymes, contain an approximately 300‐residue CP catalytic domain, have greatest amino acid sequence identity to the exocrine pancreatic enzymes CPA and CPB, and prefer hydrophobic or basic residues. They function in the breakdown of peptides in food or in other physiological processes ranging from inflammation to fibrinolysis. Members of the N/E group cleave C‐terminal basic residues and are not produced as inactive proenzymes but contain an approximately 80‐residue region following the 300‐residue CP domain with structural homology to transthyretin. They act either extra‐ or intracellularly in the processing of peptide hormones and neurotransmitters and other physiologically relevant peptides. The tertiary folding of CPs corresponds to the α/β hydrolase fold and is formed by a central mixed parallel/antiparallel eight‐strand β‐sheet, with a 120° twist between the first and the last strand, over which eight α‐helices pack on both sides to form a globular molecule. All of the enzymatically active CPs bind one atom of Zn 2+ at the active site. Some members of the CP family that are inactive against standard CP substrates lack some of the cation‐binding ligands and may therefore not be able to bind the metal.

show abstract

Rat peritoneal mast cell carboxypeptidase: localization, purification, and enzymatic properties

Cited by 74 publications

References 21 publications

Human mast cell carboxypeptidase. Purification and characterization.

Human mast cell carboxypeptidase. Purification and characterization.

Cloning and characterization of the novel gene for mast cell carboxypeptidase A.

Metallocarboxypeptidases

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