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Cx is a member of the family of connexin genes that encode the proteins of gap junction intercellular channels. Cx proteins in one cell form hemi-channels in the plasma membrane. Hemi-channels in adjacent cells dock to form complete intercellular channels through which ions and small molecules diffuse from cell to cell. Distinct Cx mutations were identified in three different families, F1, F2 and F3, affected by the same disease. To study their functional properties, normal (wild type, wt) and mutant (m) Cx proteins were expressed in cultured cells. Translation of the proteins was checked (Fig. 3). A extracellular membrane intracellular N TM 1 F1 EC 1 2 F2 3 EC 2 4 F3 AQU B 42 kDa C 42 kDa 35 kDa m-F1 Control wt PM C PM C PM C Western blot anti-Cx Control wt m-F1 PM C PM C PM C Metabolically labelled m-F2 PM C m-F2 PM C ——— m-F3 PM C m-F3 PM C Fig. 3 (A). Membrane topology of Cx protein indicating positions of mutations. Cx is an integral membrane protein with 4 transmembrane (TM) domains, two extracellular loops (EC1 and EC2) involved in hemichannel docking, and intracellular N- and C-termini. Black circles indicate the positions of mutations in families F1-F3. (B)-(C). Translation of wild type and mutant Cx proteins. mRNAs coding for wild type Cx protein (wt) and mutant Cx proteins (m-F1, m-F2, m-F3) were expressed individually in cultured cells. Plasma membrane (PM) and cytosolic (C) fractions of these cells and control cells (no Cx expressed) were run on polyacrylamide gels and the presence of Cx protein analysed using two approaches. In (B) the fractions were analysed by Western blot using an anti-Cx antibody. In (C) Cx proteins were metabolically labelled by incorporation of a radioactive amino acid during translation and detected by exposing the gels to X-ray film. 3. Describe and interpret the data in Fig. 3. You should consider what the data suggest about the type of mutation found in the three families (F1-F3) and should present an explanation for the different pattern of bands seen in (B) and (C).

Cx is a member of the family of connexin genes that encode the proteins of gap junction intercellular channels. Cx proteins in one cell form hemi-channels in the plasma membrane. Hemi-channels in adjacent cells dock to form complete intercellular channels through which ions and small molecules diffuse from cell to cell. Distinct Cx mutations were identified in three different families, F1, F2 and F3, affected by the same disease. To study their functional properties, normal (wild type, wt) and mutant (m) Cx proteins were expressed in cultured cells. Translation of the proteins was checked (Fig. 3). A extracellular membrane intracellular N TM 1 F1 EC 1 2 F2 3 EC 2 4 F3 AQU B 42 kDa C 42 kDa 35 kDa m-F1 Control wt PM C PM C PM C Western blot anti-Cx Control wt m-F1 PM C PM C PM C Metabolically labelled m-F2 PM C m-F2 PM C ——— m-F3 PM C m-F3 PM C Fig. 3 (A). Membrane topology of Cx protein indicating positions of mutations. Cx is an integral membrane protein with 4 transmembrane (TM) domains, two extracellular loops (EC1 and EC2) involved in hemichannel docking, and intracellular N- and C-termini. Black circles indicate the positions of mutations in families F1-F3. (B)-(C). Translation of wild type and mutant Cx proteins. mRNAs coding for wild type Cx protein (wt) and mutant Cx proteins (m-F1, m-F2, m-F3) were expressed individually in cultured cells. Plasma membrane (PM) and cytosolic (C) fractions of these cells and control cells (no Cx expressed) were run on polyacrylamide gels and the presence of Cx protein analysed using two approaches. In (B) the fractions were analysed by Western blot using an anti-Cx antibody. In (C) Cx proteins were metabolically labelled by incorporation of a radioactive amino acid during translation and detected by exposing the gels to X-ray film. 3. Describe and interpret the data in Fig. 3. You should consider what the data suggest about the type of mutation found in the three families (F1-F3) and should present an explanation for the different pattern of bands seen in (B) and (C).

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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Cx is a member of the family of connexin genes that encode the proteins of gap junction intercellular channels. Cx proteins in one cell form hemi-channels in the plasma membrane. Hemi-channels in adjacent cells dock to form complete intercellular channels through which ions and small molecules diffuse from cell to cell. Distinct Cx mutations were identified in three different families, F1, F2 and F3, affected by the same disease. To study their functional properties, normal (wild type, wt) and mutant (m) Cx proteins were expressed in cultured cells. Translation of the proteins was checked (Fig. 3). A extracellular EC 1 SM TM 1 membrane 2 3 4 F10 intracellular N F2 EC 2 F3 oricand c B 42 kDa C 42 kDa 35 kDa Control wt m-F1 m-F2 PM C PM C PM C PM C Western blot anti-Cx Control wt PM C m-F1 PM C PM C = Metabolically labelled m-F2 PM C m-F3 PM C m-F3 PM C WSEY Fig. 3 mont (A). Membrane topology of Cx protein indicating positions of mutations. Cx is an integral membrane protein with 4 transmembrane (TM) domains, two extracellular loops (EC1 and EC2) involved in hemichannel docking, and intracellular N- and C-termini. Black circles indicate the positions of mutations in families F1-F3. (B)-(C). Translation of wild type and mutant Cx proteins. mRNAs coding for wild type Cx protein (wt) and mutant Cx proteins (m-F1, m-F2, m-F3) were expressed individually in cultured cells. Plasma membrane (PM) and cytosolic (C) fractions of these cells and control cells (no Cx expressed) were run on polyacrylamide gels and the presence of Cx protein analysed using two approaches. In (B) the fractions were analysed by Western blot using an anti-Cx antibody. In (C) Cx proteins were metabolically labelled by incorporation of a radioactive amino acid during translation and detected by exposing the gels to X-ray film. 3. Describe and interpret the data in Fig. 3. You should consider what the data suggest about the type of mutation found in the three families (F1-F3) and should present an explanation for the different pattern of bands seen in (B) and (C). 4
Transcribed Image Text:Cx is a member of the family of connexin genes that encode the proteins of gap junction intercellular channels. Cx proteins in one cell form hemi-channels in the plasma membrane. Hemi-channels in adjacent cells dock to form complete intercellular channels through which ions and small molecules diffuse from cell to cell. Distinct Cx mutations were identified in three different families, F1, F2 and F3, affected by the same disease. To study their functional properties, normal (wild type, wt) and mutant (m) Cx proteins were expressed in cultured cells. Translation of the proteins was checked (Fig. 3). A extracellular EC 1 SM TM 1 membrane 2 3 4 F10 intracellular N F2 EC 2 F3 oricand c B 42 kDa C 42 kDa 35 kDa Control wt m-F1 m-F2 PM C PM C PM C PM C Western blot anti-Cx Control wt PM C m-F1 PM C PM C = Metabolically labelled m-F2 PM C m-F3 PM C m-F3 PM C WSEY Fig. 3 mont (A). Membrane topology of Cx protein indicating positions of mutations. Cx is an integral membrane protein with 4 transmembrane (TM) domains, two extracellular loops (EC1 and EC2) involved in hemichannel docking, and intracellular N- and C-termini. Black circles indicate the positions of mutations in families F1-F3. (B)-(C). Translation of wild type and mutant Cx proteins. mRNAs coding for wild type Cx protein (wt) and mutant Cx proteins (m-F1, m-F2, m-F3) were expressed individually in cultured cells. Plasma membrane (PM) and cytosolic (C) fractions of these cells and control cells (no Cx expressed) were run on polyacrylamide gels and the presence of Cx protein analysed using two approaches. In (B) the fractions were analysed by Western blot using an anti-Cx antibody. In (C) Cx proteins were metabolically labelled by incorporation of a radioactive amino acid during translation and detected by exposing the gels to X-ray film. 3. Describe and interpret the data in Fig. 3. You should consider what the data suggest about the type of mutation found in the three families (F1-F3) and should present an explanation for the different pattern of bands seen in (B) and (C). 4
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