Synthesis and processing of the dimorphic forms of rat α2u-globulin

Bandana Chatterjee, Nalini M. Motwani, Arun K. Roy

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Original languageEnglish
Pages (from-to)22-28
Number of pages7
JournalBBA - Gene Structure and Expression
Volume698
Issue number1
DOIs
StatePublished - Jul 30 1982
Externally publishedYes

Fingerprint

Globulins
Rats
Messenger RNA
Liver
Processing
Xenopus
Oocytes
Sprague Dawley Rats
Membranes
Cell-Free System
Reticulocytes
Inbred F344 Rats
Androgens
Polyacrylamide Gel Electrophoresis
Pancreas
Hepatocytes
Glycoproteins
Urine
Dogs
Cell membranes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology
  • Medicine(all)

Cite this

Synthesis and processing of the dimorphic forms of rat α2u-globulin. / Chatterjee, Bandana; Motwani, Nalini M.; Roy, Arun K.

In: BBA - Gene Structure and Expression, Vol. 698, No. 1, 30.07.1982, p. 22-28.

Research output: Contribution to journalArticle

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title = "Synthesis and processing of the dimorphic forms of rat α2u-globulin",
abstract = "α2u-Globulin, the androgen-dependent male rat urinary protein, can be resolved into two distinct molecular forms by SDS-polyacrylamide slab gel electrophoresis. These two forms designated as α2uA (Mr 18 800) and α2uB (Mr 18 100) are found both in urine and in the liver cells. Translation of rat liver mRNA in the rabbit reticulocyte lysate produced two preprotein forms of α2u-globulin, designated as α2uA′ (Mr 20 300) an α2uB′ (Mr 19 600). Cell-free translation of rat liver mRNA in the presence of dog pancreas microsomal membrane or in Xenopus oocytes produced the two processed forms of α2u-globulin (α2uA and α2uB). Quantitation of α2uA and α2uB within the in vitro translation products of the hepatic mRNA from albino rats of Yale, Sprague-Dawley and Fischer strains showed genetic differences in the proportion of translatable mRNA for α2uA and α2uB. The ratio of α2uA: α2uB in the translation products of rats was found to be 1:2.5 while in the case of both Sprague-Dawley and Fischer rats, the ratio was 1:4. A small portion of the α2uA and α2uB synthesized in the cultured hepatocytes, in the Xenopus oocytes or in the membrane-supplemented cell-free system appeared as two additional forms, designated as α2uA′ (Mr 21 200) and α2uB′ (Mr 20 600). Unlike α2uA and α2uB both α2uA′ and α2uB′ were found to bind to Con A-Sepharose, suggesting their glycoprotein nature.",
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AU - Roy, Arun K.

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N2 - α2u-Globulin, the androgen-dependent male rat urinary protein, can be resolved into two distinct molecular forms by SDS-polyacrylamide slab gel electrophoresis. These two forms designated as α2uA (Mr 18 800) and α2uB (Mr 18 100) are found both in urine and in the liver cells. Translation of rat liver mRNA in the rabbit reticulocyte lysate produced two preprotein forms of α2u-globulin, designated as α2uA′ (Mr 20 300) an α2uB′ (Mr 19 600). Cell-free translation of rat liver mRNA in the presence of dog pancreas microsomal membrane or in Xenopus oocytes produced the two processed forms of α2u-globulin (α2uA and α2uB). Quantitation of α2uA and α2uB within the in vitro translation products of the hepatic mRNA from albino rats of Yale, Sprague-Dawley and Fischer strains showed genetic differences in the proportion of translatable mRNA for α2uA and α2uB. The ratio of α2uA: α2uB in the translation products of rats was found to be 1:2.5 while in the case of both Sprague-Dawley and Fischer rats, the ratio was 1:4. A small portion of the α2uA and α2uB synthesized in the cultured hepatocytes, in the Xenopus oocytes or in the membrane-supplemented cell-free system appeared as two additional forms, designated as α2uA′ (Mr 21 200) and α2uB′ (Mr 20 600). Unlike α2uA and α2uB both α2uA′ and α2uB′ were found to bind to Con A-Sepharose, suggesting their glycoprotein nature.

AB - α2u-Globulin, the androgen-dependent male rat urinary protein, can be resolved into two distinct molecular forms by SDS-polyacrylamide slab gel electrophoresis. These two forms designated as α2uA (Mr 18 800) and α2uB (Mr 18 100) are found both in urine and in the liver cells. Translation of rat liver mRNA in the rabbit reticulocyte lysate produced two preprotein forms of α2u-globulin, designated as α2uA′ (Mr 20 300) an α2uB′ (Mr 19 600). Cell-free translation of rat liver mRNA in the presence of dog pancreas microsomal membrane or in Xenopus oocytes produced the two processed forms of α2u-globulin (α2uA and α2uB). Quantitation of α2uA and α2uB within the in vitro translation products of the hepatic mRNA from albino rats of Yale, Sprague-Dawley and Fischer strains showed genetic differences in the proportion of translatable mRNA for α2uA and α2uB. The ratio of α2uA: α2uB in the translation products of rats was found to be 1:2.5 while in the case of both Sprague-Dawley and Fischer rats, the ratio was 1:4. A small portion of the α2uA and α2uB synthesized in the cultured hepatocytes, in the Xenopus oocytes or in the membrane-supplemented cell-free system appeared as two additional forms, designated as α2uA′ (Mr 21 200) and α2uB′ (Mr 20 600). Unlike α2uA and α2uB both α2uA′ and α2uB′ were found to bind to Con A-Sepharose, suggesting their glycoprotein nature.

KW - (Rat)

KW - Androgenic induction

KW - mRNA translation

KW - Preprotein processing

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KW - α-Globulin

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