Protease activity of normal and PHA stimulated human lymphocytes

Arthur I. Grayzel; Victor B. Hatcher; Gerald S. Lazarus

doi:10.1016/0008-8749(75)90049-0

Protease activity of normal and PHA stimulated human lymphocytes

Arthur I. Grayzel, Victor B. Hatcher, Gerald S. Lazarus

Biochemistry

Research output: Contribution to journal › Article › peer-review

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Abstract

An assay measuring the release of TCA soluble radioactive peptides from ³H acetylated casein or hemoglobin has been used to demonstrate that human peripheral blood lymphocytes contain a number of proteases, including cathepsin D, a neutral serine protease(s) inhibited by DFP and TLCK and probably a thiol protease(s) as well. We have also found a neutral protease activity bound to the surface of the lymphocyte, but not secreted into the medium which is not inhibited by TLCK. TLCK inhibits blast transformation to PHA under conditions that do not profoundly affect protein synthesis and inhibits the total extractable proteolytic activity of lymphocytes by approximately 25%. Lymphocytes contain one or more proteases that may play a role in blast transformation and other lymphocyte functions.

Original language	English (US)
Pages (from-to)	210-219
Number of pages	10
Journal	Cellular Immunology
Volume	18
Issue number	1
DOIs	https://doi.org/10.1016/0008-8749(75)90049-0
State	Published - Jul 1975

ASJC Scopus subject areas

Immunology

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@article{4f9850fbfa3d46e095327c9d52988b88,

title = "Protease activity of normal and PHA stimulated human lymphocytes",

abstract = "An assay measuring the release of TCA soluble radioactive peptides from 3H acetylated casein or hemoglobin has been used to demonstrate that human peripheral blood lymphocytes contain a number of proteases, including cathepsin D, a neutral serine protease(s) inhibited by DFP and TLCK and probably a thiol protease(s) as well. We have also found a neutral protease activity bound to the surface of the lymphocyte, but not secreted into the medium which is not inhibited by TLCK. TLCK inhibits blast transformation to PHA under conditions that do not profoundly affect protein synthesis and inhibits the total extractable proteolytic activity of lymphocytes by approximately 25%. Lymphocytes contain one or more proteases that may play a role in blast transformation and other lymphocyte functions.",

author = "Grayzel, {Arthur I.} and Hatcher, {Victor B.} and Lazarus, {Gerald S.}",

note = "Funding Information: 1 Supported in part by Grants from the National Institutes of Health ROl-AM 17370-01 and the New York Chapter of the Arthritis Foundation. 2 Senior Investigator of the Arthritis Foundation. s Abbreviations used in this paper: TLCK, N-n-tosyl-r.-lysyl chloromethyl ketone ; PHA, phytohemagglutinin ; TCA, trichloroacetic acid ; DFP, diisopropylfluorophosphate ; NEM, N-ethylmaleimide ; FBS, fetal bovine serum.",

year = "1975",

month = jul,

doi = "10.1016/0008-8749(75)90049-0",

language = "English (US)",

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pages = "210--219",

journal = "Cellular Immunology",

issn = "0008-8749",

publisher = "Academic Press Inc.",

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T1 - Protease activity of normal and PHA stimulated human lymphocytes

AU - Grayzel, Arthur I.

AU - Hatcher, Victor B.

AU - Lazarus, Gerald S.

N1 - Funding Information: 1 Supported in part by Grants from the National Institutes of Health ROl-AM 17370-01 and the New York Chapter of the Arthritis Foundation. 2 Senior Investigator of the Arthritis Foundation. s Abbreviations used in this paper: TLCK, N-n-tosyl-r.-lysyl chloromethyl ketone ; PHA, phytohemagglutinin ; TCA, trichloroacetic acid ; DFP, diisopropylfluorophosphate ; NEM, N-ethylmaleimide ; FBS, fetal bovine serum.

PY - 1975/7

Y1 - 1975/7

N2 - An assay measuring the release of TCA soluble radioactive peptides from 3H acetylated casein or hemoglobin has been used to demonstrate that human peripheral blood lymphocytes contain a number of proteases, including cathepsin D, a neutral serine protease(s) inhibited by DFP and TLCK and probably a thiol protease(s) as well. We have also found a neutral protease activity bound to the surface of the lymphocyte, but not secreted into the medium which is not inhibited by TLCK. TLCK inhibits blast transformation to PHA under conditions that do not profoundly affect protein synthesis and inhibits the total extractable proteolytic activity of lymphocytes by approximately 25%. Lymphocytes contain one or more proteases that may play a role in blast transformation and other lymphocyte functions.

AB - An assay measuring the release of TCA soluble radioactive peptides from 3H acetylated casein or hemoglobin has been used to demonstrate that human peripheral blood lymphocytes contain a number of proteases, including cathepsin D, a neutral serine protease(s) inhibited by DFP and TLCK and probably a thiol protease(s) as well. We have also found a neutral protease activity bound to the surface of the lymphocyte, but not secreted into the medium which is not inhibited by TLCK. TLCK inhibits blast transformation to PHA under conditions that do not profoundly affect protein synthesis and inhibits the total extractable proteolytic activity of lymphocytes by approximately 25%. Lymphocytes contain one or more proteases that may play a role in blast transformation and other lymphocyte functions.

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DO - 10.1016/0008-8749(75)90049-0

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VL - 18

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JO - Cellular Immunology

JF - Cellular Immunology

IS - 1

ER -

Protease activity of normal and PHA stimulated human lymphocytes

Abstract

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