Blood-Group and Forssman Antigenic Determinants Shared between Microbes and Mammalian Cells (Part 1 of 3)

1971 ◽  
pp. 9-29 ◽  
Author(s):  
G.F. Springer
Keyword(s):  
Blood Group ◽  
Mammalian Cells ◽  
Antigenic Determinants

Synthesis of βDGlcNAc(1 →6) and βDGal(1 → 4)βDGlcNAc(1 → 6) derivatives of the TN (αDGalNAc) human blood group determinant

1982 ◽  
Vol 60 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Raymond U. Lemieux ◽  
Maria Halina Burzynska
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Antigenic Determinants ◽  
Immunological Properties ◽  
Human Blood Group ◽  
Chloride Method ◽  
Derivatives Of

In order to investigate the immunological properties of certain I blood group specific glycoproteins, the potential antigenic determinants βDGlcNAc(1 → 6)αDGalNAc and βDGal(1 → 4)βDGlcNAc(1 → 6)αDGalNAc attached as glycosides to 8-methoxy-carbonyloctanol were synthesized by way of the phthalimido-chloride method.

BLOOD GROUP AND HUMAN DISEASES (REVIEW OF LITERATURE)

2020 ◽  
Vol 65 (4) ◽  
pp. 216-221
Author(s):  
Frida Nasyrovna Gilmiyarova ◽  
N. A. Kolotyeva ◽  
V. I. Kuzmicheva ◽  
O. A. Gusyakova ◽  
I. A. Borodina ◽  
...  
Keyword(s):  
Blood Group ◽  
Gastrointestinal Diseases ◽  
Antigenic Determinants ◽  
Blood Group Antigens ◽  
Oral Diseases ◽  
Group Type ◽  
Pathological Conditions ◽  
Definition Of ◽  
Meta Analyses

AB0 blood group antigens were discovered over a century ago; however, it is still important to study their role in development of various pathological conditions. Today it is known that antigenic determinants of this blood group are present not only on erythrocyte membrane but also on other cells and tissues: platelets, gastrointestinal epithelium and salivary glands, respiratory system cells. In the last decade, a large number of studies have appeared to reveal the relationship between a specific disease and blood group type, meta-analyses have been published. Previously, the authors have studied the metabolic status, cell composition and coagulation profile of clinically healthy individuals for more than on 180,000 donations, that allowed to identify group-specific features for each blood group. This review presents generalized data on the association of such pathological conditions as coronary heart disease, thromboembolic complications, tumors of various localizations, inflammatory and destructive oral diseases, psychiatric and some infectious diseases with the presence or absence of antigenic determinants A and B. Carriers of blood group 0 (I) are generally more resistant to diseases, with the exception of H.pylori-associated gastrointestinal diseases. Carriers of «antigenic» blood groups A (II), B (III), AB (IV) are more susceptible to development of infectious, cardiovascular and cancer diseases. The presented data demonstrate clinical significance of the definition of group typing not only for selection of blood and its components during transfusion and transplantation, but also for diagnostics, determination of risk group and tactics for treatment patients with different nosologies.

scholarly journals Antipeptide antiserum identifies a widely distributed cellular tyrosine kinase related to but distinct from the c-fps/fes-encoded protein.

1986 ◽  
Vol 6 (4) ◽  
pp. 1065-1073 ◽  
Author(s):  
R A Feldman ◽  
J P Tam ◽  
H Hanafusa
Keyword(s):  
Tyrosine Kinase ◽  
Mammalian Cells ◽  
Adult Life ◽  
Kinase Domain ◽  
Cellular Protein ◽  
Antigenic Determinants ◽  
Protein Kinase Activity ◽  
Normal Cells ◽  
Cellular Homolog ◽  
Sarcoma Virus

We raised antibodies directed against a synthetic peptide representing an amino acid sequence of the conserved kinase domain of the transforming protein of Fujinami sarcoma virus (FSV) (P140). The antiserum obtained specifically recognized FSV-P140 and its cellular homolog and in addition, it recognized a new cellular protein of 94,000 daltons (NCP94) in avian and mammalian cells. NCP94 was found to be associated with a cyclic nucleotide-independent protein kinase activity that was specific for tyrosine residues. Although NCP94 and FSV-P140 share antigenic determinants, NCP94 is not a cellular homolog of FSV-P140: NCP94 and the previously identified c-fps/fes product were different in their tryptic fingerprints and in their tissue specificities. Thus, the function of NCP94 in normal cells is probably different than that of the c-fps/fes product. NCP94 was expressed in every tissue and cell line that was examined. In chickens, NCP94 levels were highest during embryonic development and NCP94 expression was high in gizzard, brain, and spleen throughout embryonic and adult life. The universal expression of NCP94 suggests that this protein may be involved in an essential function of normal cells. NCP94 may be a new cellular tyrosine kinase of the src gene family.

scholarly journals Three types of blood group I specificity among monoclonal anti-I autoantibodies revealed by analogues of a branched erythrocyte glycolipid.

1979 ◽  
Vol 149 (4) ◽  
pp. 975-980 ◽  
Author(s):  
T Feizi ◽  
R A Childs ◽  
K Watanabe ◽  
S I Hakomori
Keyword(s):  
Sialic Acid ◽  
Blood Group ◽  
Antigenic Determinants ◽  
The Third ◽  
Group I

Blood group I activities of the purified glycosphingolipid lacto-N-iso-octaosyl ceramide (Fromula: see text) and 8 of its analogues have been evaluated with 11 anti-I sera including 5 anti-I sera previously tested. All but one of the antisera were inhibited by the lacto-N-iso-octaosyl structure. Three types of I-specificity could be distinguished although none of the anti-I sera was identical in its inhibition patterns with the nine glycophingolipid analogues. The anti-I sera Ma and Woj represent the first type and require an intact Galbeta1 leads to 4GlcNAcbeta1 leads to 6 chain, the anti-I sera Step, Gra, Ver, and Ful represent the second type which requires Galbeta1 leads to 4GlcNAcbeta1 leads to 3 chain with branching, and the anti-I sera Phi, Da, Sch, and Low belong to the third type which requires both branches to be intact. Anti-I antibodies varry in their ability to react with their antigenic determinants in the presence of external substitutions with alpha-linked galactose or sialic acid.

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