Purification and partial characterization of aminopeptidase A from the serum of pregnant and non-pregnant women

Lalu, Kaisa; Lampelo, Saara; Nummelin-Kortelainen, Monica; Vanha‐Perttula, T.

doi:10.1016/0167-4838(84)90188-2

Cited by 40 publications

(18 citation statements)

References 20 publications

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“…Purification of APA to homogeneity with these tissue sources is complicated by the relative abundance of other structurally related enzymes and lack of a specific antibody (19,20,(22)(23)(24)(25). The relatively high expression levels of the BP-1/6C3 antigen on transformed pre-B cells has allowed its purification, sequence analysis, and cDNA cloning (11).…”

Section: Discussionmentioning

confidence: 99%

“…There are two forms of APA-a membrane-bound form on cell surfaces and a soluble form present in serum (12,22,25,27). The two forms could be encoded by different genes, but more likely they are products ofthe same gene, since they are very similar in molecular characteristics, substrate specificity, pH profile, and activation by alkaline earth metals (20).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3.

Cooper

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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The predicted amino acid sequence of the cDNA encoding the murine B-lymphocyte differentiation antigen BP-1/6C3 suggested that it is a member of the zincdependent metalloprotease family, possibly an aminopeptidase related to aminopeptidase N [microsomal aminopeptidase; a-aminoacyl-peptide hydrolase (microsomal), EC 3. (refs. 4-6; unpublished results).While its broad tissue distribution implied diverse biological function, studies of the BP-1/6C3 antigen thus far have been focused mainly on its possible role in B lymphocyte development. The BP-1/6C3 molecule is expressed on pre-B and immature B-lineage cells in the bone marrow (2, 3, 7), and its expression on stromal cell lines correlates with their ability to support pre-B-cell growth (4). Moreover, interleukin 7 (IL-7) preferentially induces BP-1/6C3 expression together with pre-B-cell proliferation (6, 8) and up-regulated expression of the BP-1/6C3 antigen, which is often seen on transformed pre-B cells (1, 2, 9, 10).In an effort to define the structure and function of this interesting cell-surface molecule, we purified the antigen and cloned its cDNA from an Abelson murine leukemia virustransformed pre-B-cell line (11). The amino acid sequence predicted from the cDNA sequence suggested that the murine BP-1/6C3 antigen is a member of the zinc-dependent metalloprotease family, possibly an aminopeptidase related to aminopeptidase N [APN; microsomal aminopeptidase; a-aminoacyl-peptide hydrolase (microsomal) EC 3.4.11.2]. Four distinctive types of aminopeptidases have been reported (12). These include APN, which has a relatively broad specificity acting on peptides with an N-terminal neutral amino acid; aminopeptidase A [APA; u-a-aspartyl(L-a-glutamyl)-peptide hydrolase, EC 3.4.11.7], acting on peptides with N-terminal acidic amino acids; aminopeptidase P (aminoacrylprolyl-peptide hydrolase, EC 3.4.11.9) and aminopeptidase W, which hydrolyze peptides in which the penultimate amino acid is a proline or a tryptophan.In the present studies, we have obtained evidence that the BP-1/6C3-reactive molecule exhibits APA activity.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3.

Cooper

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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“…In contrast with the highly basic pH optimum of AHE, other aminopeptidases A are most active at neutral [Il,12,[16][17][18]241 or slightly basic pH [13, 251. AHE is completely inhibited by chelating agents. Some inhibitors of serine proteases also show strong inhibitory effects, but high concentrations of inhibitors were needed to cause complete inhibition.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an aminopeptidase A fromStaphylococcus chromogenesand its use for the synthesis of amino‐acid derivatives and dipeptides

Yoshpe-Besancon

Auriol²,

Paul³

et al. 1993

European Journal of Biochemistry

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An aminopeptidase with original specificity was purified 3800-fold to homogeneity from a cellular extract of Staphylococcus chromogenes. The enzyme was specific for acidic amino acids (Asp and Glu) at the N-terminus of peptides and thus can be classified as an aminopeptidase A. However, its specificity was not restricted to acidic amino acids: a-hydroxy acids such as L-malic and L-lactic acids were also accepted in position P1. The enzyme had a broad specificity for the residue at position P' 1, accepting all types of amino acids, including Pro, in this position. The optimal conditions for the hydrolysis of Asp-Phe-NHz were pH 9.5 and 60°C. The enzyme was inhibited by chelating agents and serine-protease inhibitors. The activity lost by treatment with chelating agents could be restored by Mn2+ or Znzf which also stimulated the native enzyme. This suggests that it is a metalloprotease with a serine residue essential for the activity. The native enzyme had an apparent molecular mass of 430 kDa on gradient-gel electrophoresis and subunits of 43 kDa as determined by SDS/PAGE. The enzyme catalyzed the synthesis of peptide and amino acid derivatives such as Asp-Phe-OMe (Aspartame) and malyl-Tyr-OEt from L -A s~ and L-malic acid as acyl donors and L-Phe-OMe and LTyr-OEt as nucleophiles, respectively. The use of the enzyme as a reagent in protease-catalyzed peptide synthesis, N-terminal protection and subsequent deprotection, is described.

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“…Peptidases such as aminopeptidase A are present in serum 3 and can demonstrate variable concentrations dependant on clinical conditions. For example, aminopeptidase A is at higher levels in pregnant women than in nonpregnant women.…”

Section: Introductionmentioning

confidence: 99%

“…For example, aminopeptidase A is at higher levels in pregnant women than in nonpregnant women. 3 To further complicate matters, there is a difference in both the activity and amount of serum proteolytic enzymes dependent on species, resulting in differential metabolism of both peptide and nonpeptide drugs. 4,5 The metabolic stability of bradykinin and [des-Arg9] bradykinin in serum show marked species difference.…”

Section: Introductionmentioning

confidence: 99%

Development of neuropeptide drugs that cross the blood-brain barrier

Egleton

Davis

2005

Neurotherapeutics

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Purification and partial characterization of aminopeptidase A from the serum of pregnant and non-pregnant women

Cited by 40 publications

References 20 publications

Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3.

Aminopeptidase A activity of the murine B-lymphocyte differentiation antigen BP-1/6C3.

Purification and characterization of an aminopeptidase A fromStaphylococcus chromogenesand its use for the synthesis of amino‐acid derivatives and dipeptides

Development of neuropeptide drugs that cross the blood-brain barrier

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