Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice.

نویسندگان

  • M Estela Campanella
  • Haiyan Chu
  • Nancy J Wandersee
  • Luanne L Peters
  • Narla Mohandas
  • Diana M Gilligan
  • Philip S Low
چکیده

Previous research has shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human erythrocyte membranes. Because GE binding sites have been mapped to sequences on the membrane protein, band 3, that are not conserved in other mammalian homologs, the question arose whether GEs can organize into complexes on other mammalian erythrocyte membranes. To address this, murine erythrocytes were stained with antibodies to glyceraldehyde-3-phosphate dehydrogenase, aldolase, phosphofructokinase, lactate dehydrogenase, and pyruvate kinase and analyzed by confocal microscopy. GEs were found to localize to the membrane in oxygenated erythrocytes but redistributed to the cytoplasm upon deoxygenation, as seen in human erythrocytes. To identify membrane proteins involved in GE assembly, erythrocytes from mice lacking each of the major erythrocyte membrane proteins were examined for GE localization. GEs from band 3 knockout mice were not membrane associated but distributed throughout the cytoplasm, regardless of erythrocyte oxygenation state. In contrast, erythrocytes from mice lacking alpha-spectrin, ankyrin, protein 4.2, protein 4.1, beta-adducin, or dematin headpiece exhibited GEs bound to the membrane. These data suggest that oxygenation-dependent assembly of GEs on the membrane could be a general phenomenon of mammalian erythrocytes and that stability of these interactions depends primarily on band 3.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Characterization of Glycolytic Enzyme Interactions with Murine Erythrocyte Membranes in Wild type and Membrane Protein Knockout Mice Short title for the running head: GLYCOLYTIC ENZYME INTERACTIONS WITH ERYTHROCYTE MEMBRANES

Previous research has shown that glycolytic enzymes (GEs) exist as multi-enzyme complexes on the inner surface of human erythrocyte membranes. Because GE binding sites have been mapped to sequences on the membrane protein, band 3, that are not conserved in other mammalian homologs, the question arose whether GEs can organize into complexes on other mammalian erythrocyte membranes. To address th...

متن کامل

Deletion of histidine decarboxylase (HDC) enhances the antinociceptive effects of orexin A in the central nervous system

It has long been established that histamine plays a role as a mediator of inflammation. From numerous studies, it has been well known that the amine has many pharmacological actions on a variety of organs. To evaluate the role of histamine in pain perception, we generated HDC knockout mice using a gene targeting method. Histamine is a hydrophilic autacoid, and in most tissues it is stored and s...

متن کامل

Deletion of histidine decarboxylase (HDC) enhances the antinociceptive effects of orexin A in the central nervous system

It has long been established that histamine plays a role as a mediator of inflammation. From numerous studies, it has been well known that the amine has many pharmacological actions on a variety of organs. To evaluate the role of histamine in pain perception, we generated HDC knockout mice using a gene targeting method. Histamine is a hydrophilic autacoid, and in most tissues it is stored and s...

متن کامل

Roles of the Duffy antigen and glycophorin A in malaria infectionand erythrocyte.

We constructed gene knockout mice lacking either the Duffy antigen (Dfy) or glycophorin A (GPA), major glycoproteins that are expressed on erythrocyte membranes, to examine the role of these proteins in malaria infection and erythrocyte. All of the rodent malarias examined proliferated in the erythrocytes of these knockout mice, indicating that neither the Duffy antigen nor GPA has an essential...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Blood

دوره 112 9  شماره 

صفحات  -

تاریخ انتشار 2008