Ontogenetic changes in hemoglobin synthesis of two strains of Chironomus tentans

Development ◽  
1969 ◽  
Vol 22 (3) ◽  
pp. 465-476
Author(s):  
Darrel S. English
Keyword(s):  
Molecular Weight ◽  
Serum Protein ◽  
Human Blood ◽  
Protein Analysis ◽  
Chironomus Tentans ◽  
Ontogenetic Changes ◽  
Hemoglobin Synthesis ◽  
Chironomus Plumosus ◽  
Monomeric Structure ◽  
Chironomus Thummi

Differentiating cells can be characterized by the number and types of proteins they produce (Markert, 1963). In man and other organisms the diversity of hemoglobins has been correlated with ontogenetic changes which reflect the alterations of gene activity (Ingram, 1963). Furthermore, the types of proteins produced are generally specific for the species. The study of insect coelomic proteins has followed closely that of mammalian serum protein analysis; however, profound differences exist between human blood and insect coelomic fluids. For this reason, the term ‘hemolymph’, rather than blood, has been used to designate these fluids. Svedberg & Eriksson-Quensal (1934) first studied the ultracentrifuge properties of Chironomus plumosus hemoglobins and determined them to have a molecular weight of 34000. Braunitzer & Braun (1965) described the multiplicity of hemoglobins in Chironomus thummi and claimed two subunits per molecule. Manwell (1966) suggested the hemoglobins of Chironomus plumosus possessed a monomeric structure.

Porous membrane strip microsampling: a dried biofluid collection format and application for quantitative enzyme immunoassay

2016 ◽  
Vol 8 (24) ◽  
pp. 4835-4843 ◽  
Author(s):  
Jeanne V. Samsonova ◽  
Anastasia D. Chadina ◽  
Alexander P. Osipov ◽  
Sergey E. Kondakov
Keyword(s):  
Molecular Weight ◽  
Blood Serum ◽  
Enzyme Immunoassay ◽  
High Molecular Weight ◽  
Human Blood ◽  
Porous Membrane ◽  
Human Blood Serum ◽  
Membrane Strip

Applicability of a new and simple membrane-strip microsampling format for the analysis of human blood serum in a strip-dried form for the presence of a range of model low and high molecular weight analytes by ELISA was demonstrated.

Serum Protein Corona Abolishes Changes in the Expression of Proinflammatory Genes Induced by Quantum Dots in Human Blood Mononuclear Cell

2020 ◽  
Vol 169 (1) ◽  
pp. 95-99
Author(s):  
D. V. Novikov ◽  
S. G. Selivanova ◽  
N. V. Krasnogorova ◽  
E. N. Gorshkova ◽  
S. N. Pleskova ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Mononuclear Cell ◽  
Serum Protein ◽  
Human Blood ◽  
Protein Corona

scholarly journals Regulation of interleukin-6 expression in cultured human blood monocytes and monocyte-derived macrophages

Blood ◽  
1988 ◽  
Vol 72 (4) ◽  
pp. 1134-1140 ◽  
Author(s):  
J Bauer ◽  
U Ganter ◽  
T Geiger ◽  
U Jacobshagen ◽  
T Hirano ◽  
...  
Keyword(s):  
Molecular Weight ◽  
B Cell ◽  
Human Blood ◽  
Interleukin 6 ◽  
Interferon Beta ◽  
Interleukin 2 ◽  
Mononuclear Phagocytes ◽  
Blood Monocytes ◽  
Beta 2 ◽  
Stimulatory Factor

Abstract A culture system that allows human blood monocytes to differentiate into macrophages in vitro was used to study B-cell stimulatory factor- 2/interleukin-6 (interferon-beta 2/26 kd protein) expression in mononuclear phagocytes. Using B-cell stimulatory factor-2 (BSF-2) cDNA and a polyclonal, monospecific antibody directed against human BSF-2, we find that strong interleukin-6 (IL-6) expression is initiated in cultured monocytes on stimulation with endotoxin. Maximally induced monocytic BSF-2/IL-6 synthesis (1% to 2% of total proteins secreted by monocytes) is more than ten times stronger than in terminally differentiated macrophages (approximately 0.1% of total secretory proteins). BSF-2/IL-6 mRNA was detectable as early as one hour after stimulation with endotoxin, reaching maximum levels three hours after stimulus. Interleukin-1 (IL-1) was able to stimulate IL-6 synthesis in monocytes, but not in macrophages. Tumor necrosis factor, interferon- gamma and interleukin-2 (IL-2) had no effect on IL-6 synthesis in monocytes or macrophages. We found five molecular weight forms of BSF- 2/IL-6 to be secreted by monocytes of 21.5 kd, 23.5 kd, 24 kd, 26 kd, and 28 kd apparent molecular weight. The 26 kd and 28 kd forms were found to represent N-glycosylated molecules, which were not detectable on treatment of the cells with the N-glycosylation inhibitor tunicamycin. The 21.5 kd, 23.5 kd, and 24 kd BSF-2/IL-6 forms were unaffected by tunicamycin treatment. We conclude from our data that cells of the mononuclear phagocyte lineage are one of the main sites of BSF-2/IL-6 (interferon-beta 2/26 kd protein/HSF) synthesis.

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