scholarly journals PGE2 enhances Ca2+‐dependent ionic currents in the airway mucus gland cells

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Huiling Liu ◽  
Bela Kanyicska ◽  
Jerry M Farley
2018 ◽  
Vol 103 (11) ◽  
pp. 1543-1559 ◽  
Author(s):  
Shunichi Gamo ◽  
Tsutomu Tamada ◽  
Koji Murakami ◽  
Soshi Muramatsu ◽  
Hidemi Aritake ◽  
...  

Author(s):  
R. B. Clark

One of the puzzling features of polychaetes and some other animals is the tendency for epidermal mucus cells to become incorporated into the central nervous system (Clark, 1966). In a number of species of Nephtys an extensive prostomial mucus gland system has come into close association with the supraoesophageal ganglion of which it sometimes forms two enormous posterior lobes (Clark, 1955, 1958). Cells which are comparable to, if not homologous with, those in Nephtys are even more completely incorporated into the supraoesophageal ganglion of nereids (Bobin & Durchon, 1953; Durchon & Frezal, 1955; Hauenschild & Fischer, 1962; Herlant-Meewis & Van Damme, 1962) and glycerids (Simpson, 1959), though, unlike the situation in nephtyids, the connexion between these cells and the exterior is tenuous or even problematical in nereids and glycerids. In Pisione, superficial gland cells near the median ocelli of the trochophore larva are incorporated into the supraoesophageal ganglion at metamorphosis and form two well-defined glandular masses near the posterior eyes in the adult, losing their ducts to the exterior in the process, but retaining the appearance of gland cells (Åkesson, 1961).


Author(s):  
Peter Heffernan

This work reports on the fine structure and histochemistry of several regions of the alimentary canal in Pholoe minuta (Fabricius, 1780). Particular emphasis is placed on the elaborate secretory cells (tryptophan-containing secretion) associated with the pharyngeal jaws. Mucus gland cells were located and described for the oesophagus (acid mucins), pharynx papillae (sulphated acid mucins), pharynx luminal lining (mixed acid mucins) and the intestine (mixed acid mucins). Enzymic gland cells (zymogen-like secretory granules) were identified in the luminal lining of the pharynx and in the intestine. Lysosome-containing cells (presumably absorptive) were described in the intestine. Glycogen reserves were observed along the coelomic peritoneum and a seasonal pattern for their deposition and utilization is briefly discussed.


2021 ◽  
Vol 22 (2) ◽  
pp. 687
Author(s):  
Tong Zhou ◽  
Bolan Zhou ◽  
Yasong Zhao ◽  
Qing Li ◽  
Guili Song ◽  
...  

Most currently available bioreactors have some defects in the expression, activity, or purification of target protein and peptide molecules, whereas the mucus gland of fish can overcome these defects to become a novel bioreactor for the biopharmaceutical industry. In this study, we have evaluated the practicability of developing a mucus gland bioreactor in loach (Paramisgurnus dabryanus). A transgenic construct pT2-krt8-IFN1 was obtained by subcloning the promoter of zebrafish keratin 8 gene and the type I interferon (IFN1) cDNA of grass carp into the SB transposon. The IFN1 expressed in CIK cells exhibited an antiviral activity against the replication of GCRV873 and activated two genes downstream of JAK-STAT signaling pathway. A transgenic loach line was then generated by microinjection of the pT2-krt8-IFN1 plasmids and in vitro synthesized capped SB11 mRNA. Southern blots indicated that a single copy of IFN1 gene was stably integrated into the genome of transgenic loach. The expression of grass carp IFN1 in transgenic loaches was detected with RT-PCR and Western blots. About 0.0825 µg of grass carp IFN1 was detected in 20 µL mucus from transgenic loaches. At a viral titer of 1 × 103 PFU/mL, plaque numbers on plates containing mucus from transgenic loaches reduced by 18% in comparison with those of the control, indicating that mucus of IFN1-transgenic loaches exhibited an antiviral activity. Thus, we have successfully created a mucus gland bioreactor that has great potential for the production of various proteins and peptides.


Sign in / Sign up

Export Citation Format

Share Document