Tissue-specific secretory proteins of the salivary glands of Chironomus thummi An electrophoretic and immunochemical analysis

Chromosoma ◽  
1985 ◽  
Vol 92 (4) ◽  
pp. 283-289 ◽  
Author(s):  
E. P. Kopantzev ◽  
E. I. Karakin ◽  
I. I. Kiknadze
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins ◽  
Immunochemical Analysis ◽  
Tissue Specific ◽  
Chironomus Thummi

Cell-specific synthesis and glycosylation of secretory proteins in larval salivary glands of Chironomus thummi

Chromosoma ◽  
1981 ◽  
Vol 83 (5) ◽  
pp. 661-677 ◽  
Author(s):  
N. N. Kolesnikov ◽  
E. I. Karakin ◽  
Tamara E. Sebeleva ◽  
L. Meyer ◽  
E. Serfling
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins ◽  
Chironomus Thummi ◽  
Specific Synthesis

Secretory proteins and Balbiani ring gene activities in salivary glands of Chironomus thummi larvae

Chromosoma ◽  
1983 ◽  
Vol 88 (1) ◽  
pp. 16-23 ◽  
Author(s):  
E. Serfling ◽  
L. Meyer ◽  
A. Rudolph ◽  
Kerstin Steiner
Keyword(s):  
Salivary Glands ◽  
Secretory Proteins ◽  
Balbiani Ring ◽  
Chironomus Thummi

scholarly journals Tissue-specific expression in the salivary glands of transgenic mice

1992 ◽  
Vol 20 (9) ◽  
pp. 2249-2255 ◽  
Author(s):  
Thomas R. Mikkelsen ◽  
Jakob Brandt ◽  
H.Jakob Larsen ◽  
Birte B. Larsen ◽  
Knud Poulsen ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Salivary Glands ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression

scholarly journals Dynamic tracking and identification of tissue-specific secretory proteins in the circulation of live mice

2020 ◽  
Author(s):  
Jae Myoung Suh ◽  
Kwang-eun Kim ◽  
Isaac Park ◽  
Jeesoo Kim ◽  
Myeong-Gyun Kang ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Mouse Liver ◽  
Secretory Pathway ◽  
Secretory Protein ◽  
Protein Labeling ◽  
Secretory Proteins ◽  
Tissue Specific ◽  
Dynamic Tracking

Abstract Here we describe iSLET (in situ Secretory protein Labeling via ER-anchored TurboID) which labels secretory pathway proteins as they transit through the ER-lumen to enable dynamic tracking of tissue-specific secreted proteomes in vivo. We expressed iSLET in the mouse liver and demonstrated efficient in situ labeling of the liver-specific secreted proteome which could be tracked and identified within circulating blood plasma. iSLET is a versatile and powerful tool for studying spatiotemporal dynamics of secretory proteins, a valuable class of biomarkers and therapeutic targets.

scholarly journals THE ORIENTATION OF DNA WITHIN 80-ANGSTROM CHROMATIN FIBERS

1972 ◽  
Vol 52 (3) ◽  
pp. 639-647 ◽  
Author(s):  
David B. Dusenbery ◽  
Robert B. Uretz
Keyword(s):  
Electron Microscope ◽  
Fluorescence Microscopy ◽  
Salivary Glands ◽  
Acridine Orange ◽  
Average Thickness ◽  
Polarized Fluorescence ◽  
Chromatin Fibers ◽  
The Individual ◽  
Dna Packing ◽  
Chironomus Thummi

Squashing salivary glands of Chironomus thummi larvae, Amblystoma tigrinum erythrocytes, or Spirostromum frequently results in stretched chromatin having highly oriented DNA as determined by polarized fluorescence microscopy of acridine orange-stained preparations. The examination of such material from C. thummi in the electron microscope indicates that the individual chromatin fibers have an average thickness of 80 A as is usually found in embedded and sectioned material. It is thus concluded that the DNA lies nearly parallel to the axis of these chromatin fibers. Detailed calculations of the polarization expected from various models of DNA packing are contained in an appendix.

scholarly journals Comparative developmental analysis of the parotid, submandibular and sublingual glands in the neonatal rat

1982 ◽  
Vol 204 (3) ◽  
pp. 673-679 ◽  
Author(s):  
M G Humphreys-Beher ◽  
D L Hollis ◽  
D M Carlson
Keyword(s):  
Salivary Glands ◽  
Submandibular Gland ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Neonatal Rat ◽  
Leucine Incorporation ◽  
Sublingual Gland ◽  
Neonatal Development ◽  
Glycoprotein Synthesis ◽  
Tissue Specific

Analysis of the soluble protein fractions from the rat parotid, submandibular and sublingual glands by polyacrylamide-gel electrophoresis reveals similarities in overall patterns of protein synthesis at birth. Tissue-specific changes in protein and glycoprotein synthesis occur shortly after birth and again at the time of weaning, 21-28 days later. Incorporation of [3H]thymidine into DNA was at its highest after birth and gradually decreased in both the parotid and submandibular gland, whereas [3H]thymidine incorporation in the sublingual gland was low throughout the time of neonatal development. [14C]Leucine incorporation into total protein increased in all glands with age after birth, showing an accelerated rate 21-28 days later. Trichloroacetic acid/phosphotungstic acid-precipitable [3H]fucose in glycoproteins declined over the time of neonatal development in the parotid and submandibular gland, but its incorporation remained higher in the sublingual gland. alpha-Amylase (EC 3.2.1.1) in the salivary glands increased at the time of weaning, as judged by detectability in sodium dodecyl sulphate/polyacrylamide gels and by immune precipitation. Two membrane-bound enzymes, UDP-galactose:2-acetamido-2-deoxy-D-glucosamine 4 β-galactosyltransferase (EC 2.4.1.22) and UDP-galactose:2-acetamido-2-deoxy-D-galactosaminyl-protein 3 β-galactosyltransferase (no EC number), undergo tissue-specific change rather than changes induced by physiological stimulation of the salivary glands.

A tissue-specific puff (Balbiani ring a) in Chironomus thummi may contain a gene encoding a 67-kDa protein which exhibits non-tissue-specific expression

Gene ◽  
1990 ◽  
Vol 96 (2) ◽  
pp. 241-247 ◽  
Author(s):  
S.S. Bogachev ◽  
A.G. Blinov ◽  
N.N. Kolesnikov ◽  
S.V. Scherbik ◽  
A.V. Taranin ◽  
...  
Keyword(s):  
Balbiani Ring ◽  
Gene Encoding ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression ◽  
Chironomus Thummi

scholarly journals Transcriptomic Analysis of Salivary Glands of Ornithodoros brasiliensis Aragão, 1923, the Agent of a Neotropical Tick-Toxicosis Syndrome in Humans

2021 ◽  
Vol 12 ◽  
Author(s):  
Jose Reck ◽  
Anelise Webster ◽  
Bruno Dall’Agnol ◽  
Ronel Pienaar ◽  
Minique H. de Castro ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Secretory Protein ◽  
Clinical Findings ◽  
Host Responses ◽  
Secretory Proteins ◽  
Major Protein ◽  
Host Interaction ◽  
Salivary Gland Protein ◽  
Duplication Events ◽  
Tick Salivary Glands

Tick salivary glands produce and secrete a variety of compounds that modulate host responses and ensure a successful blood meal. Despite great progress made in the identification of ticks salivary compounds in recent years, there is still a paucity of information concerning salivary molecules of Neotropical argasid ticks. Among this group of ticks, considering the number of human cases of parasitism, including severe syndromes and hospitalization, Ornithodoros brasiliensis can be considered one of the major Neotropical argasid species with impact in public health. Here, we describe the transcriptome analysis of O. brasiliensis salivary glands (ObSG). The transcriptome yielded ~14,957 putative contigs. A total of 368 contigs were attributed to secreted proteins (SP), which represent approximately 2.5% of transcripts but ~53% expression coverage transcripts per million. Lipocalins are the major protein family among the most expressed SP, accounting for ~16% of the secretory transcripts and 51% of secretory protein abundance. The most expressed transcript is an ortholog of TSGP4 (tick salivary gland protein 4), a lipocalin first identified in Ornithodoros kalahariensis that functions as a leukotriene C4 scavenger. A total of 55 lipocalin transcripts were identified in ObSG. Other transcripts potentially involved in tick-host interaction included as: basic/acid tail secretory proteins (second most abundant expressed group), serine protease inhibitors (including Kunitz inhibitors), 5' nucleotidases (tick apyrases), phospholipase A2, 7 disulfide bond domain, cystatins, and tick antimicrobial peptides. Another abundant group of proteins in ObSG is metalloproteases. Analysis of these major protein groups suggests that several duplication events after speciation were responsible for the abundance of redundant compounds in tick salivary glands. A full mitochondrial genome could be assembled from the transcriptome data and confirmed the close genetic identity of the tick strain sampled in the current study, to a tick strain previously implicated in tick toxicoses. This study provides novel information on the molecular composition of ObSG, a Brazilian endemic tick associated with several human cases of parasitism. These results could be helpful in the understanding of clinical findings observed in bitten patients, and also, could provide more information on the evolution of Neotropical argasids.

scholarly journals The M33 Chemokine Receptor Homolog of Murine Cytomegalovirus Exhibits a Differential Tissue-Specific Role during In Vivo Replication and Latency

2009 ◽  
Vol 83 (15) ◽  
pp. 7590-7601 ◽  
Author(s):  
Rhonda D. Cardin ◽  
Gregory C. Schaefer ◽  
Janelle R. Allen ◽  
Nicholas J. Davis-Poynter ◽  
Helen E. Farrell
Keyword(s):  
Salivary Glands ◽  
Specific Role ◽  
Murine Cytomegalovirus ◽  
Wild Type Virus ◽  
Pcr Analysis ◽  
Wild Type ◽  
Viral Dna ◽  
Mcmv Infection ◽  
Tissue Specific

ABSTRACT M33, encoded by murine cytomegalovirus (MCMV), is a member of the UL33 homolog G-protein-coupled receptor (GPCR) family and is conserved across all the betaherpesviruses. Infection of mice with recombinant viruses lacking M33 or containing specific signaling domain mutations in M33 results in significantly diminished MCMV infection of the salivary glands. To determine the role of M33 in viral dissemination and/or infection in other tissues, viral infection with wild-type K181 virus and an M33 mutant virus, ΔM33BT2, was characterized using two different routes of inoculation. Following both intraperitoneal (i.p.) and intranasal (i.n.) inoculation, M33 was attenuated for infection of the spleen and pancreas as early as 7 days after infection. Following i.p. inoculation, ΔM33BT2 exhibited a severe defect in latency as measured by a diminished capacity to reactivate from spleens and lungs in reactivation assays (P < 0.001). Subsequent PCR analysis revealed markedly reduced ΔM33BT2 viral DNA levels in the latently infected spleens, lungs, and bone marrow. Following i.n. inoculation, latent ΔM33BT2 viral DNA was significantly reduced in the spleen and, in agreement with results from i.p. inoculation, did not reactivate from the spleen (P < 0.001). Furthermore, in vivo complementation of ΔM33BT2 virus replication and/or dissemination to the salivary glands and pancreas was achieved by coinfection with wild-type virus. Overall, our data suggest a critical tissue-specific role for M33 during infection in the salivary glands, spleen, and pancreas but not the lungs. Our data suggest that M33 contributes to the efficient establishment or maintenance of long-term latent MCMV infection.

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