Instability of Red Cell Shape Associated with the Absence of Membrane Glycophorin C

Candace A. Kuczmarski; Armando R. Orlina; Lauri K. Delahanty; Edward R. Kuczmarski

doi:10.1111/j.1423-0410.1987.tb02986.x

Instability of Red Cell Shape Associated with the Absence of Membrane Glycophorin C

Candace A. Kuczmarski^*, Armando R. Orlina, Lauri K. Delahanty, Edward R. Kuczmarski

^*Corresponding author for this work

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

4 Scopus citations

Abstract

Abstract. Erythocytes from 3 Gerbich‐negative siblings readily converted to echinocytes when subjected to changing concentrations of sodium or lithium chloride. When erythrocyte membrane proteins were assayed by immunoblotting with human anti‐Ge 1,2, normal membranes were found to contain a reactive component of an approximate molecular weight of 33,000 daltons which was absent from the Gerbich‐negative individuals. PAS staining and mobility on SDS gels identified this component as glycophorin C. These observations indicate that glyocophorin C (β‐sialoglycoprotein) is a component of the Gerbich antigen and is involved in normal cell shape maintenance.

Original language	English (US)
Pages (from-to)	36-42
Number of pages	7
Journal	Vox Sanguinis
Volume	52
Issue number	1-2
DOIs	https://doi.org/10.1111/j.1423-0410.1987.tb02986.x
State	Published - Mar 1987
Externally published	Yes

ASJC Scopus subject areas

Hematology

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10.1111/j.1423-0410.1987.tb02986.x

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title = "Instability of Red Cell Shape Associated with the Absence of Membrane Glycophorin C",

abstract = "Abstract. Erythocytes from 3 Gerbich‐negative siblings readily converted to echinocytes when subjected to changing concentrations of sodium or lithium chloride. When erythrocyte membrane proteins were assayed by immunoblotting with human anti‐Ge 1,2, normal membranes were found to contain a reactive component of an approximate molecular weight of 33,000 daltons which was absent from the Gerbich‐negative individuals. PAS staining and mobility on SDS gels identified this component as glycophorin C. These observations indicate that glyocophorin C (β‐sialoglycoprotein) is a component of the Gerbich antigen and is involved in normal cell shape maintenance.",

author = "Kuczmarski, {Candace A.} and Orlina, {Armando R.} and Delahanty, {Lauri K.} and Kuczmarski, {Edward R.}",

year = "1987",

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doi = "10.1111/j.1423-0410.1987.tb02986.x",

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journal = "Vox Sanguinis",

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T1 - Instability of Red Cell Shape Associated with the Absence of Membrane Glycophorin C

AU - Kuczmarski, Candace A.

AU - Orlina, Armando R.

AU - Delahanty, Lauri K.

AU - Kuczmarski, Edward R.

PY - 1987/3

Y1 - 1987/3

N2 - Abstract. Erythocytes from 3 Gerbich‐negative siblings readily converted to echinocytes when subjected to changing concentrations of sodium or lithium chloride. When erythrocyte membrane proteins were assayed by immunoblotting with human anti‐Ge 1,2, normal membranes were found to contain a reactive component of an approximate molecular weight of 33,000 daltons which was absent from the Gerbich‐negative individuals. PAS staining and mobility on SDS gels identified this component as glycophorin C. These observations indicate that glyocophorin C (β‐sialoglycoprotein) is a component of the Gerbich antigen and is involved in normal cell shape maintenance.

AB - Abstract. Erythocytes from 3 Gerbich‐negative siblings readily converted to echinocytes when subjected to changing concentrations of sodium or lithium chloride. When erythrocyte membrane proteins were assayed by immunoblotting with human anti‐Ge 1,2, normal membranes were found to contain a reactive component of an approximate molecular weight of 33,000 daltons which was absent from the Gerbich‐negative individuals. PAS staining and mobility on SDS gels identified this component as glycophorin C. These observations indicate that glyocophorin C (β‐sialoglycoprotein) is a component of the Gerbich antigen and is involved in normal cell shape maintenance.

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JO - Vox Sanguinis

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ER -

Instability of Red Cell Shape Associated with the Absence of Membrane Glycophorin C

Abstract

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