Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

[Tamm-Horsfall protein].

M N Peraldi1

  • 1Service de Néphrologie A, Hôpital Tenon, Paris.

Nephrologie
|January 1, 1992
PubMed
Summary
This summary is machine-generated.

Tamm-Horsfall (TH) glycoprotein, a major urinary protein, shares homology with rat pancreatic protein GP2. Further research into this protein family may elucidate TH protein's physiological and pathological roles.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

French ENT Society (SFORL) guidelines for the management of immunodeficient patients with head and neck cancer of cutaneous origin.

European annals of otorhinolaryngology, head and neck diseases·2014
Same author

[20% of living donor kidney transplantation in France? Yes, it's possible!].

Nephrologie & therapeutique·2013
Same author

Renal transplantation in HIV-infected patients: the Paris experience.

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons·2010
Same author

Nephron sparing surgery is a feasible and efficient treatment of T1a renal cell carcinoma in kidney transplant: a prospective series from a single center.

The Journal of urology·2008
Same author

[Indications of central venous access in the context of acute renal insufficiency].

Nephrologie·2002
Same author

[Physiopathology of the nephropathy associated with HIV virus infection].

Nephrologie·2001
Same journal

Short-term effect of folic acid supplementation in renal transplant recipients and chronic kidney disease patients with comparable renal function impairment.

Nephrologie·2004
Same journal

[Acute renal failure and 2,8-dihydroxyadeninuria].

Nephrologie·2004
Same journal

[Phototherapy and hemodialysis pruritus].

Nephrologie·2004
Same journal

[Pregnancy and hemodialysis].

Nephrologie·2004
Same journal

[Role of dietary fibers in the nutritional management of chronic renal failure].

Nephrologie·2004
Same journal

[Abstracts of the VI Meeting of the Society of Nephrology and of the Francophone Society of Dialysis. Marseille, France, 28 September-1 October 2004].

Nephrologie·2004
See all related articles

Area of Science:

  • Nephrology
  • Biochemistry
  • Urology

Background:

  • Tamm-Horsfall (TH) glycoprotein is a major protein found in normal urine and is the primary component of waxy nephron casts.
  • It originates from the kidney, specifically localized in the thick ascending limb of the loop of Henle and distal convoluted tubule.
  • TH glycoprotein exhibits physicochemical properties including aggregation in response to increasing NaCl or H+ concentrations.

Purpose of the Study:

  • To characterize the primary structure and properties of Tamm-Horsfall (TH) glycoprotein.
  • To investigate the relationship between TH glycoprotein and uromodulin.
  • To explore potential roles and regulation mechanisms of TH protein in physiological and pathological conditions.

Main Methods:

  • Characterization of the primary structure of Tamm-Horsfall (TH) glycoprotein.

Related Experiment Videos

  • Comparison of TH glycoprotein with uromodulin and rat pancreatic protein GP2.
  • Localization studies within the renal tubules.

    • Main Results:

    • The primary structure of TH glycoprotein is identical to uromodulin, though glycosylation differs, affecting immunosuppressive properties.
    • TH protein is anchored to the cytoplasmic membrane via a phosphatidyl-inositol group and may be secreted after phospholipase cleavage.
    • Significant homology (88%) was found between TH protein and rat pancreatic protein GP2.

    Conclusions:

    • TH glycoprotein and uromodulin share structural identity but differ in glycosylation and associated functions.
    • The discovery of homologous proteins like GP2 suggests a potential protein family that could aid in understanding TH protein's function.
    • The precise physiological and pathological roles and regulatory mechanisms of TH protein remain largely unknown and warrant further investigation.