Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.

Mogens Holst Nissen; Ole Jannik Bjerrum; T Plesner; M Wilken; M Rørth

Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.

Mogens Holst Nissen, Ole Jannik Bjerrum, T Plesner, M Wilken, M Rørth

29 Citations (Scopus)

Abstract

Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.

Original language	English
Journal	Clinical and Experimental Immunology
Volume	67
Issue number	2
Pages (from-to)	425-32
Number of pages	7
ISSN	0009-9104
Publication status	Published - 1987

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@article{e55c5710ba3511ddae57000ea68e967b,

title = "Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.",

abstract = "Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.",

author = "Nissen, {Mogens Holst} and Bjerrum, {Ole Jannik} and T Plesner and M Wilken and M R{\o}rth",

note = "Keywords: Carcinoma, Small Cell; Endopeptidases; Humans; Hydrogen-Ion Concentration; Immunoelectrophoresis, Two-Dimensional; Lung Neoplasms; Protease Inhibitors; Serine Endopeptidases; Temperature; beta 2-Microglobulin",

year = "1987",

language = "English",

volume = "67",

pages = "425--32",

journal = "Clinical and Experimental Immunology",

issn = "0009-9104",

publisher = "Wiley-Blackwell",

number = "2",

}

TY - JOUR

T1 - Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.

AU - Nissen, Mogens Holst

AU - Bjerrum, Ole Jannik

AU - Plesner, T

AU - Wilken, M

AU - Rørth, M

N1 - Keywords: Carcinoma, Small Cell; Endopeptidases; Humans; Hydrogen-Ion Concentration; Immunoelectrophoresis, Two-Dimensional; Lung Neoplasms; Protease Inhibitors; Serine Endopeptidases; Temperature; beta 2-Microglobulin

PY - 1987

Y1 - 1987

N2 - Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.

AB - Modification of beta-2-microglobulin has been shown to occur in vitro in serum of patients suffering of small cell lung cancer, where it clearly correlated to the clinical course of disease. The cause of serum beta-2-microglobulin modification occurring in these patients is investigated in the present study. This revealed that modification of beta-2-microglobulin is due to cleavage by a serine protease, which is dependent on divalent cations and has a trypsin-like specificity. The process showed the following characteristics: pH optimum at 8.5, heat inactivation by incubation at 56 degrees C for 20 min and temperature optimum at 20 degrees C.

M3 - Journal article

C2 - 3038438

SN - 0009-9104

VL - 67

SP - 425

EP - 432

JO - Clinical and Experimental Immunology

JF - Clinical and Experimental Immunology

IS - 2

ER -

Modification of beta-2-microglobulin in sera from patients with small cell lung cancer: evidence for involvement of a serine protease.

Abstract

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