The gene organization of the human β7 subunit, the common β subunit of the leukocyte integrins HML-1 and LPAM-1

1992 ◽  
Vol 4 (9) ◽  
pp. 1031-1040 ◽  
Author(s):  
Wei-Meng Jiang ◽  
David Jenkins ◽  
Qian Yuan ◽  
Euphemia Leung ◽  
K. H. Andy Choo ◽  
...  
Keyword(s):  
Gene Organization ◽  
Β Subunit ◽  
Leukocyte Integrins ◽  
The Common

scholarly journals Identification of a Novel Two-Partner Secretion Locus in Moraxella catarrhalis

2007 ◽  
Vol 75 (6) ◽  
pp. 2929-2936 ◽  
Author(s):  
Pascale Plamondon ◽  
Nicole R. Luke ◽  
Anthony A. Campagnari
Keyword(s):  
Moraxella Catarrhalis ◽  
Amino Acid Level ◽  
Peptide Sequencing ◽  
Gene Organization ◽  
Open Reading Frames ◽  
Bronchial Epithelial ◽  
Liquid Chromatography Tandem Mass ◽  
Normal Human ◽  
The Common ◽  
Culture Supernatants

ABSTRACT Although Moraxella catarrhalis continues to be a significant cause of disease in both children and adults, the steps involved in pathogenesis remain poorly understood. We have identified three open reading frames in the M. catarrhalis genome that encode homologues of the two-partner secretion system (TPS). The sequenced M. catarrhalis hemagglutinin-like locus of strain 7169 has a unique gene organization composed in the order of mchA1, mchB, and mchA2, where mchA1 is divergent. MchA1 and MchA2 are 74% identical at the amino acid level and diverge only in the C-terminal regions. The TPS motif identified in the common N-terminal regions of MchA1 and MchA2 was found to be homologous to the filamentous hemagglutinin of Bordetella pertussis, and MchB has homology to other TpsB transporters. The presence of MchA1 and MchA2 in outer membrane protein preparations and concentrated culture supernatants (CCSs) of strain 7169 was confirmed by immunoblotting using specific antisera. Nanoscale liquid chromatography-tandem mass spectrometry peptide sequencing of the antibody-reactive bands from the CCSs was performed and demonstrated that 13 different peptides mapped to identical regions of MchA1 and MchA2. Quantitative adherence assays revealed a decrease of binding to primary normal human bronchial epithelial cells by the mch mutants 7169mchB and 7169mchA1A2B compared to that by the wild-type strain. These studies show that MchA1, MchA2, and MchB are components of a novel TPS identified in M. catarrhalis and suggest that these proteins may be involved in colonization.

scholarly journals Structure of the Complete Extracellular Domain of the Common β Subunit of the Human GM-CSF, IL-3, and IL-5 Receptors Reveals a Novel Dimer Configuration

Cell ◽  
2001 ◽  
Vol 104 (2) ◽  
pp. 291-300 ◽  
Author(s):  
Paul D. Carr ◽  
Sonja E. Gustin ◽  
Alice P. Church ◽  
James M. Murphy ◽  
Sally C. Ford ◽  
...  
Keyword(s):  
Extracellular Domain ◽  
Β Subunit ◽  
Gm Csf ◽  
The Common

scholarly journals Deciphering site 3 interactions of interleukin 12 and interleukin 23 with their cognate murine and human receptors

2020 ◽  
Vol 295 (30) ◽  
pp. 10478-10492 ◽  
Author(s):  
Alessandra Esch ◽  
Anna Masiarz ◽  
Sofie Mossner ◽  
Jens M. Moll ◽  
Joachim Grötzinger ◽  
...  
Keyword(s):  
Interleukin 12 ◽  
Receptor Complex ◽  
Β Subunit ◽  
Α Subunit ◽  
Binding Interface ◽  
Human Ortholog ◽  
The Common ◽  
Interleukin 23

Interleukin (IL)–12 and IL-23 belong to the IL-12 type family and are composite cytokines, consisting of the common β subunit p40 and the specific cytokine α subunit p35 and p19, respectively. IL-12 signals via the IL-12Rβ1·IL-12Rβ2 receptor complex, and IL-23 uses also IL-12Rβ1 but engages IL-23R as second receptor. Importantly, binding of IL-12 and IL-23 to IL-12Rβ1 is mediated by p40, and binding to IL-12Rβ2 and IL-23R is mediated by p35 and p19, respectively. Previously, we have identified a W157A substitution at site 3 of murine IL-23p19 that abrogates binding to murine IL-23R. Here, we demonstrate that the analogous Y185R site 3 substitution in murine and Y189R site 3 substitution in human IL-12p35 abolishes binding to IL-12Rβ2 in a cross-species manner. Although Trp157 is conserved between murine and human IL-23p19 (Trp156 in the human ortholog), the site 3 W156A substitution in hIL-23p19 did not affect signaling of cells expressing human IL-12Rβ1 and IL-23R, suggesting that the interface of murine IL-23p19 required for binding to IL-23R is different from that in the human ortholog. Hence, we introduced additional hIL-23p19 substitutions within its binding interface to hIL-23R and found that the combined site 3 substitutions of W156A and L160E, which become buried at the complex interface, disrupt binding of hIL-23p19 to hIL-23R. In summary, we have identified substitutions in IL-12p35 and IL-23p19 that disrupt binding to their cognate receptors IL-12Rβ2 and IL-23R in a murine/human cross-species manner.

Levels of α-subunits of gonadotropins can be increased in Zollinger-Ellison syndrome, both in patients with malignant tumours and with apparently benign disease

1988 ◽  
Vol 118 (1) ◽  
pp. 135-141 ◽  
Author(s):  
Linda Bardram ◽  
Tove Agner ◽  
Claus Hagen
Keyword(s):  
Malignant Disease ◽  
Molecular Form ◽  
Tumour Marker ◽  
Benign Disease ◽  
Tumour Resection ◽  
Β Subunit ◽  
Malignant Tumours ◽  
Α Subunit ◽  
Zollinger Ellison Syndrome ◽  
The Common

Abstract. To evaluate the value of intact hCG, the β-subunit of hCG and the common α-subunit of the glycoprotein hormones as tumour markers in patients with gastrinomas, we investigated 30 patients with the Zollinger-Ellison syndrome. Fifty-seven percent of the patients with malignant disease (N = 7) and 45% of those with active and apparently benign disease (N = 20) had raised values of circulating α-subunit. Detectable levels of hCG or hCG-β were found in 7 patients of whom 4 had malignant disease. Radical tumour resection in 2 patients resulted in normalisation of elevated levels of β-subunit, and in one patient who developed metastases, the α-subunit values became elevated simultaneously. By chromatographic studies we found that the α-subunit-like reacting substance in serum eluted as the normal free α-subunit in 8 patients, but in one patient with metastatic disease we found evidence for production of a larger molecular form of α-subunit. The results indicate that the common α-subunit is a valuable tumour marker in patients with gastrinomas, whereas hCG-β is only seldomly elevated. Single estimates of any of the hormonal fragments seem not to relate with malignancy, whereas a rise in α-subunit concentration in some patients may be related to the development of malignancy.

Regulation of α and thyrotrophin-β subunit mRNA levels by androgens in the female rat

1990 ◽  
Vol 5 (1) ◽  
pp. 1-6 ◽  
Author(s):  
J. A. O. Ahlquist ◽  
J. A. Franklyn ◽  
D. B. Ramsden ◽  
M. C. Sheppard
Keyword(s):  
Thyroid Hormones ◽  
Mrna Levels ◽  
Female Rat ◽  
Β Subunit ◽  
Similar Reduction ◽  
Subunit Mrna ◽  
Genes Encoding ◽  
The Common ◽  
Influence Gene Expression ◽  
Serum Tsh

ABSTRACT Thyroid and steroid hormones act by similar mechanisms to influence gene expression in the anterior pituitary gland. The genes encoding the common α and TSH-β glycoprotein subunits are known to be regulated by thyroid hormones; we report here the effects of androgen administration on levels of α and TSH-β mRNA in pituitary cytoplasm in the euthyroid and hypothyroid female rat. Dihydrotestosterone (DHT) suppressed both α and TSH-β mRNAs to levels lower than those found in untreated animals; a similar reduction was seen in hypothyroid animals treated with DHT. A biphasic response of TSH-β mRNA was seen following administration of tri-iodothyronine (T3) to hypothyroid rats, with early stimulation followed by later inhibition; these changes were also evident after administration of T3 to androgen-treated animals, although mRNA levels were again suppressed. The effects of testosterone were similar to those of DHT. In contrast to the changes in mRNA levels, androgen administration did not lead to significant alterations in serum TSH concentrations or pituitary TSH content. These results indicate that, like thyroid hormones, androgens suppress both α and TSH-β subunit mRNA levels in the female rat. Androgens, however, exert differential effects on TSH synthesis and release which contrast with those of thyroid hormones.

Function of the Common β Subunit of the GM-CSF/IL-3/IL-5 Receptors

1994 ◽  
pp. 217-223 ◽  
Author(s):  
Alice Mui ◽  
Akihiko Muto ◽  
Kazuhiro Sakamaki ◽  
Noriko Sato ◽  
Taisei Kinoshita ◽  
...  
Keyword(s):  
Β Subunit ◽  
Gm Csf ◽  
The Common

A proteolytically truncated form of free CD18, the common chain of leukocyte integrins, as a novel marker of activated myeloid cells

Blood ◽  
2001 ◽  
Vol 98 (5) ◽  
pp. 1561-1566 ◽  
Author(s):  
Karel Drbal ◽  
Pavla Angelisová ◽  
Ivan Hilgert ◽  
Jan Černý ◽  
Petr Novák ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Myeloid Cells ◽  
Peptide Sequencing ◽  
Resting Cells ◽  
Blood Monocytes ◽  
Leukocyte Integrins ◽  
Activated Neutrophils ◽  
The Common ◽  
Macrophage Colony

An unusual CD18 monoclonal antibody (mAb) MEM-148 binds, in contrast to standard CD18 mAbs, specifically to peripheral blood monocytes and neutrophils activated by various stimuli such as phorbol myristate acetate, opsonized zymosan, heat-aggregated immunoglobulin, and (after priming with lipopolysaccharide, tumor necrosis factor, or granulocyte-macrophage colony-stimulating factor) also by formyl-methionyl-leucyl-phenylalanine. In addition, in vivo activated neutrophils obtained from urine of patients following recent prostatectomy were also strongly positive for MEM-148. On the activated myeloid cells the mAb recognized a 65- to 70-kd protein identified immunochemically and by mass spectrometric peptide sequencing as a membrane-anchored fragment of CD18 (the common chain of leukocyte integrins) produced by proteolytic cleavage. The CD18 fragment originated mainly from integrin molecules stored intracellularly in resting cells, it was unassociated with CD11 chains, and its formation was inhibited by several types of protease inhibitors. Thus, the 65- to 70-kd CD18 fragment represents a novel abundant activation marker of myeloid cells of so far unknown function but possibly involved in conformational changes in leukocyte integrin molecules resulting in increased affinity to their ligands.

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