scholarly journals Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues

1994 ◽  
Vol 124 (3) ◽  
pp. 381-394 ◽  
Author(s):  
R Vuolteenaho ◽  
M Nissinen ◽  
K Sainio ◽  
M Byers ◽  
R Eddy ◽  
...  
Keyword(s):  
Primary Structure ◽  
Chain Gene ◽  
Chromosomal Assignment ◽  
Cdna Clones ◽  
Heavy Chains ◽  
Fetal Tissues ◽  
Gene Transcripts ◽  
A Chain ◽  
Human Fetal Tissues ◽  
Domain I

The primary structure of the human laminin M chain was determined from cDNA clones isolated from human placental libraries. The clones covered a total of 6,942 bp, with 49-bp encoding a 5' end untranslated region and 6,893-bp coding for a translated sequence. The complete human laminin M chain contains a 22-residue signal peptide and 3,088 residues of the mature M chain. The M chain has a domain structure similar to that of the human and mouse A chains. The homology between the two human laminin heavy chains is highest in the short arm region and lowest in the long arm helical domain I + II. Northern blot analysis of human fetal tissues showed that the M chain was expressed in most tissues such as cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain, but not in liver, thymus, and bone. In situ hybridization localized the expression of the M chain gene to cells of mesenchymal origin. In contrast, expression of the A chain was observed only in kidney, testis, neuroretina and some region of brain as determined by Northern analyses. Epithelial and endothelial cells were negative for both M and A chain gene transcripts. The gene for the human M chain (LAMM) was localized to chromosome 6q22-->23.

scholarly journals A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment.

1992 ◽  
Vol 119 (3) ◽  
pp. 679-693 ◽  
Author(s):  
P Kallunki ◽  
K Sainio ◽  
R Eddy ◽  
M Byers ◽  
T Kallunki ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chain Structure ◽  
Amino Acid Sequences ◽  
Northern Analysis ◽  
Chain Gene ◽  
Chromosomal Assignment ◽  
The Novel ◽  
Putative Signal Peptide ◽  
Human Fetal Tissues ◽  
Domain I

We describe the identification of a novel laminin chain. Overlapping clones were isolated from a human fibrosarcoma HT1080 cell cDNA library spanning a total of 5,200 bp. A second set of clones contained an alternative 3' end sequence giving a total of 4,316 bp. The longer sequence contained an open reading frame for a 1,193-residue-long polypeptide. The alternative sequence was shortened at the carboxyl-terminal end coding for a 1,111-residue-long polypeptide. The amino acid sequence contained 21 amino acids of a putative signal peptide and 1,172 residues or alternatively 1,090 residues of a sequence with five distinct domains homologous to domains I-V in laminin chains. Comparison of the amino acid sequences showed that the novel laminin chain is homologous to the laminin B2 chain. However, the structure of the novel laminin chain isolated here differs significantly from that of the B2 chain in that it has no domain VI and domains V, IV, and III are shorter, resulting in a truncated laminin chain. The alternative sequence had a shortened domain I/II. In accordance with the current nomenclature, the chain characterized here is termed B2t. Calculation of possible chain interactions of laminin chains with the B2t chain domain I/II indicated that the B2t chain can replace the B2 chain in some laminin molecules. The gene for the laminin B2t chain (LAMB2T) was localized to chromosome 1q25-q31 in close proximity to the laminin B2 chain gene. Northern analysis showed that the B2t chain is expressed in several human fetal tissues but differently from the laminin B1 and B2 chains. By in situ hybridization expression of the B2t chain was localized to specific epithelial cells in skin, lung, and kidney as opposed to a general epithelial and endothelial cell expression of the laminin B2 chain in the same tissues.

Isolation of Nuclear Fractions from Human Fetal Tissues

Pharmacology ◽  
1985 ◽  
Vol 30 (4) ◽  
pp. 188-196 ◽  
Author(s):  
G.M. Pacifici ◽  
H. Glaumann ◽  
A. Rane°
Keyword(s):  
Fetal Tissues ◽  
Human Fetal Tissues

scholarly journals Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones.

1987 ◽  
Vol 262 (36) ◽  
pp. 17757-17767 ◽  
Author(s):  
K Doege ◽  
M Sasaki ◽  
E Horigan ◽  
J R Hassell ◽  
Y Yamada
Keyword(s):  
Primary Structure ◽  
Core Protein ◽  
Cdna Clones ◽  
Cartilage Proteoglycan ◽  
Complete Primary Structure

scholarly journals Screening of potent neutralizing antibodies against SARS-CoV-2 using convalescent patients-derived phage-display libraries

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Yongbing Pan ◽  
Jianhui Du ◽  
Jia Liu ◽  
Hai Wu ◽  
Fang Gui ◽  
...  
Keyword(s):  
Phage Display ◽  
Neutralizing Antibodies ◽  
Variable Region ◽  
Neutralizing Antibody ◽  
Chain Gene ◽  
Prophylactic Efficacy ◽  
Heavy Chains ◽  
Effective Interventions ◽  
Phage Display Libraries

AbstractAs the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to threaten public health worldwide, the development of effective interventions is urgently needed. Neutralizing antibodies (nAbs) have great potential for the prevention and treatment of SARS-CoV-2 infection. In this study, ten nAbs were isolated from two phage-display immune libraries constructed from the pooled PBMCs of eight COVID-19 convalescent patients. Eight of them, consisting of heavy chains encoded by the immunoglobulin heavy-chain gene-variable region (IGHV)3-66 or IGHV3-53 genes, recognized the same epitope on the receptor-binding domain (RBD), while the remaining two bound to different epitopes. Among the ten antibodies, 2B11 exhibited the highest affinity and neutralization potency against the original wild-type (WT) SARS-CoV-2 virus (KD = 4.76 nM for the S1 protein, IC50 = 6 ng/mL for pseudoviruses, and IC50 = 1 ng/mL for authentic viruses), and potent neutralizing ability against B.1.1.7 pseudoviruses. Furthermore, 1E10, targeting a distinct epitope on RBD, exhibited different neutralization efficiency against WT SARS-CoV-2 and its variants B.1.1.7, B.1.351, and P.1. The crystal structure of the 2B11–RBD complexes revealed that the epitope of 2B11 highly overlaps with the ACE2-binding site. The in vivo experiment of 2B11 using AdV5-hACE2-transduced mice showed encouraging therapeutic and prophylactic efficacy against SARS-CoV-2. Taken together, our results suggest that the highly potent SARS-CoV-2-neutralizing antibody, 2B11, could be used against the WT SARS-CoV-2 and B.1.1.7 variant, or in combination with a different epitope-targeted neutralizing antibody, such as 1E10, against SARS-CoV-2 variants.

Maternal microchimerism in human fetal tissues

2008 ◽  
Vol 198 (3) ◽  
pp. 325.e1-325.e6 ◽  
Author(s):  
Anna Maria Jonsson ◽  
Mehmet Uzunel ◽  
Cecilia Götherström ◽  
Nikos Papadogiannakis ◽  
Magnus Westgren
Keyword(s):  
Fetal Tissues ◽  
Human Fetal Tissues
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