Common acute lymphoblastic leukemia antigen expressed on leukemia and melanoma cell lines has neutral endopeptidase activity.

Jongeneel, C. Victor; Quackenbush, Elizabeth J.; Ronco, Pierre; Verroust, P; Carrel, Stefan; Letarte, Michelle

doi:10.1172/jci113936

Cited by 55 publications

(27 citation statements)

References 47 publications

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“…Binding of iodine-125-or tritium-labeled Ang II or hllA by the anti-Ang II mAbs or a control mAb (CDV 135) specific for neutral endopeptidase 33 was tested by liquid-phase radioimmunoassay (RIA) as previously described. 31 Briefly, the radiolabeled ligand in 20 jtl phosphate-buffered saline containing 0.1% bovine serum albumin (PBS-BSA) was reacted for 1 hour at room temperature with 20 fi\ of 1:10 diluted hybridoma supernatant in the absence or the presence of hllA or Ang II.…”

Section: Binding To Anti-angiotensin II Monoclonal Antibodiesmentioning

confidence: 99%

Antagonist effect of a receptor-mimicking peptide encoded by human angiotensin II complementary RNA.

et al. 1992

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A ngiotensin II (Ang II), the final effector in the / \ renin-angiotensin system (RAS), is generated J. X . through a cascade of proteolytic reactions including cleavage of angiotensinogen by renin to release the decapeptide angiotensin I, which is further converted into Ang II by the angiotensin converting enzyme (ACE).1 In general terms, two theoretical approaches can be considered to interfere with the RAS function in the treatment of hypertension. It is first possible to decrease the production and/or extracellular concentration of Ang II. In spite of efforts to develop agents acting at the level of renin, 2 ACE inhibitors 3 constitute at present the most successful antihypertensive drugs interfering with the RAS. However, they also inhibit other actions of ACE on kinins, enkephalins, or substance P and do not decrease the production of Ang II generated locally via other enzymatic systems. 4 The

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Section: Binding To Anti-angiotensin II Monoclonal Antibodiesmentioning

confidence: 99%

Antagonist effect of a receptor-mimicking peptide encoded by human angiotensin II complementary RNA.

et al. 1992

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“…CD10 is a cell surface glycoprotein expressed in both normal and neoplastic cells, including follicular lymphoma 10) , renal cell carcinoma 11) , endometrial stromal sarcoma 11)12) , atypical fibroxanthoma 13) , and many benign or malignant tumors 11)13) , although the precise function of CD 10 in each tumor is still not fully understood 14) . CD10 expression in MM was first described by 9 Jongeneel et al 15) using flow cytometry in cell lines. Carrel et al 16)17) then showed CD10 expression in vivo in MM tissues by IHC; several other reports have significantly correlated CD10 expression levels with tumor progression 6)8) [18][19][20] .…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical CD10 Expression is Useful for Differentiating Malignant Melanoma from Benign Melanocytic Nevus

Hoshikawa

Koizumi

Handa

et al. 2015

J St. Marianna Univ

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Malignant melanoma (MM), an aggressive skin neoplasm, can be difficult to differentiate histologically from benign melanocytic nevi (BMN). Although immunohistochemical analysis could facilitate diagnosis of MM, markers that discriminate between benign and malignant lesions have not yet been established. However, CD10 expression is associated with MM progression. We immunostained 36 MM and 50 BMN specimens for CD10 to evaluate whether CD10 immunostaining could distinguish between BMN and MM tumors. In the 36 MM samples, we found CD10 expression in 17 (47.2%) sample tumor cells and 32 (88.9%) stromal cells, for 34 of the 36 MM specimens (94.4%) overall. In contrast, no BMN (0/50) samples had CD10 + tumor cells, although a few (8/50, 16.0%) showed stromal staining. The two specimen types thus significantly differed in CD10 expression (P<0.01), indicating that melanocytic CD10 + tumor cells are likely to be malignant. Also, melanocytic stromal cells with diffuse, strong CD10 expression are more likely to be malignant than those with light, focal CD10 expression. Although hematoxylin and eosin staining is fundamental to the diagnosis of melanocytic lesions, CD10 immunostaining may help distinguish between BMN and MM.

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“…In addition to those with receptor or ligand functions, others have been found to be membrane enzymes that may have important regulatory functions during B-cell maturation (1). For example, the human B-cell antigens CD10, CD45, and CD73 are enzymes possessing neutral endopeptidase, protein-tyrosine-phosphatase, and ecto-5'-nucleotidase activities, respectively (2)(3)(4). Most of the known B-cell markers are expressed during early or middle stages of B-cell ontogeny.…”

mentioning

confidence: 99%

Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1.

Rebbe

Tong

Finley

et al. 1991

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

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Common acute lymphoblastic leukemia antigen expressed on leukemia and melanoma cell lines has neutral endopeptidase activity.

Cited by 55 publications

References 47 publications

Antagonist effect of a receptor-mimicking peptide encoded by human angiotensin II complementary RNA.

Antagonist effect of a receptor-mimicking peptide encoded by human angiotensin II complementary RNA.

Immunohistochemical CD10 Expression is Useful for Differentiating Malignant Melanoma from Benign Melanocytic Nevus

Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1.

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