H and B human blood-group antigen expression in cochlear hair cells is modulated by thyroxine

1994 ◽  
Vol 276 (2) ◽  
pp. 239-243 ◽  
Author(s):  
Pablo Gil-Loyzaga ◽  
Manuel Remezal ◽  
Rosella Mollicone ◽  
Angeles Ib��ez ◽  
Rafael Oriol
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Hair Cells ◽  
Antigen Expression ◽  
Blood Group Antigen ◽  
Cochlear Hair Cells ◽  
Human Blood Group

H and B human blood-group antigen expression in cochlear hair cells is modulated by thyroxine

1994 ◽  
Vol 276 (2) ◽  
pp. 239-243
Author(s):  
Pablo Gil-Loyzaga ◽  
Manuel Remezal ◽  
Rosella Mollicone ◽  
Angeles Ib��ez ◽  
Rafael Oriol
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Hair Cells ◽  
Antigen Expression ◽  
Blood Group Antigen ◽  
Cochlear Hair Cells ◽  
Human Blood Group

Neuronal influence on B and H human blood-group antigen expression in rat cochlear cultures

1992 ◽  
Vol 269 (1) ◽  
pp. 13-20 ◽  
Author(s):  
Pablo Gil-Loyzaga ◽  
Manuel Remezal ◽  
Rafael Oriol
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Antigen Expression ◽  
Blood Group Antigen ◽  
Human Blood Group

A NEW RARE HUMAN BLOOD-GROUP ANTIGEN (Wra)

The Lancet ◽  
1953 ◽  
Vol 262 (6777) ◽  
pp. 119-120 ◽  
Author(s):  
C.A. Holman
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Blood Group Antigen ◽  
Human Blood Group

‘Heibel’ a New Rare Human Blood Group Antigen, Revealed by a Haemolytic Disease of a Newborn

Vox Sanguinis ◽  
1968 ◽  
Vol 14 (4) ◽  
pp. 307-309 ◽  
Author(s):  
L. Ballowitz ◽  
H. Fiedler ◽  
Ch. Hoffmann ◽  
H. Pettenkofer
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Blood Group Antigen ◽  
Haemolytic Disease ◽  
Human Blood Group

Prolactin antagonizes the corticoid-promoted development of adult-type epidermis in cultured larval bullfrog skin.

1996 ◽  
Vol 199 (12) ◽  
pp. 2573-2578
Author(s):  
M Takada ◽  
H Yai ◽  
S Komazaki ◽  
K Takayama-Arita
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Short Circuit ◽  
Short Circuit Current ◽  
Blood Group Antigen ◽  
Basal Cells ◽  
Adult Type ◽  
Human Blood Group ◽  
Larval Type ◽  
Antigen A

EDTA-treated larval bullfrog skin, in which apical and skein cells had been removed and only basal cells remained, was cultured in one of four media. These contained either aldosterone (Aldo) or a mixture of Aldo, hydrocortisone (HC) and corticosterone (C), each either supplemented with prolactin (PRL) or lacking PRL. Skin cultured with Aldo alone or with the corticoid mixture (Aldo + HC + C) developed an adult-type epidermis: (i) both types of skin reacted to human blood group antigen A, a marker for the adult-type epidermis of bullfrog skin; (ii) amiloride decreased the short-circuit current Isc in these skin preparations, but acetylcholine (ACh) had no effect on the Isc. It seemed to make little difference to the results whether the skin was cultured with Aldo or with the corticoid mixture. PRL antagonized the action of Aldo and induced the development of a larval-type epidermis in both skin preparations: (i) the skin preparations did not react to human blood group antigen A; (ii) acetylcholine and amiloride each stimulated Isc in these preparations. Since ACh and amiloride each stimulated the Isc in skin with apical cells, ACh/amiloride-stimulated channels may be located on these cells.

A novel I-branching β-1,6-N-acetylglucosaminyltransferase involved in human blood group I antigen expression

Blood ◽  
2003 ◽  
Vol 101 (7) ◽  
pp. 2870-2876 ◽  
Author(s):  
Niro Inaba ◽  
Toru Hiruma ◽  
Akira Togayachi ◽  
Hiroko Iwasaki ◽  
Xiao-Hui Wang ◽  
...  
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Bone Marrow Cells ◽  
Molecular Genetic ◽  
Chinese Hamster ◽  
Antigen Expression ◽  
Branching Enzyme ◽  
Exon 2 ◽  
Human Blood Group ◽  
Group I

The human blood group i and I antigens are determined by linear and branched poly-N-acetyllactosamine structures, respectively. In erythrocytes, the fetal i antigen is converted to the adult I antigen by I-branching β-1,6-N-acetylglucosaminyltransferase (IGnT) during development. Dysfunction of the I-branching enzyme may result in the adult i phenotype in erythrocytes. However, the I gene responsible for blood group I antigen has not been fully confirmed. We report here a novel human I-branching enzyme, designatedIGnT3. The genes for IGnT1 (reported in 1993),IGnT2 (also presented in this study), and IGnT3consist of 3 exons and share the second and third exons. Bone marrow cells preferentially expressed IGnT3 transcript. During erythroid differentiation using CD34+ cells,IGnT3 was markedly up-regulated with concomitant decrease in IGnT1/2. Moreover, reticulocytes expressed theIGnT3 transcript, but IGnT1/2 was below detectable levels. By molecular genetic analyses of an adult i pedigree, individuals with the adult i phenotype were revealed to have heterozygous alleles with mutations in exon 2 (1006G>A; Gly336Arg) and exon 3 (1049G>A; Gly350Glu), respectively, of the IGnT3gene. Chinese hamster ovary (CHO) cells transfected with each mutatedIGnT3 cDNA failed to express I antigen. These findings indicate that the expression of the blood group I antigen in erythrocytes is determined by a novel IGnT3, not byIGnT1 or IGnT2.

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