Cardiac amyloidosis future or investigational therapies: Difference between revisions

Jump to navigation Jump to search
Line 9: Line 9:
Possible future treatment options which are currently being investigated include:
Possible future treatment options which are currently being investigated include:
* Anti-SAP antibody
* Anti-SAP antibody
* CPHPC
* CPHPC<ref name="pmid12015594">{{cite journal|author = Pepys MB, Herbert J, Hutchinson WL, Tennent GA, Lachmann HJ, Gallimore JR, Lovat LB, Bartfai T, Alanine A, Hertel C, Hoffmann T, Jakob-Roetne R, Norcross RD, Kemp JA, Yamamura K, Suzuki M, Taylor GW, Murray S, Thompson D, Purvis A, Kolstoe S, Wood SP, Hawkins PN | title = Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis | journal = Nature | volume = 417 | issue = 6886 | pages = 254–9 | year = 2002 | pmid = 12015594 | doi = 10.1038/417254a }}</ref>
* Diflunisal<ref name="pmid17107884">{{cite journal |author=Sekijima Y, Dendle MA, Kelly JW |title=Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis |journal=[[Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis]] |volume=13 |issue=4 |pages=236–49 |year=2006 |month=December |pmid=17107884 |doi=10.1080/13506120600960882 |url=}}</ref>
* Diflunisal<ref name="pmid17107884">{{cite journal |author=Sekijima Y, Dendle MA, Kelly JW |title=Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis |journal=[[Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis]] |volume=13 |issue=4 |pages=236–49 |year=2006 |month=December |pmid=17107884 |doi=10.1080/13506120600960882 |url=}}</ref>
* Tamafidis
* Tamafidis<ref name="pmid22645360">{{cite journal |author=Bulawa CE, Connelly S, Devit M, ''et al.'' |title=Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade |journal=[[Proceedings of the National Academy of Sciences of the United States of America]] |volume=109 |issue=24 |pages=9629–34 |year=2012 |month=June |pmid=22645360 |pmc=3386102 |doi=10.1073/pnas.1121005109 |url=}}</ref>
* Eprodisate
* Eprodisate


CPHPC, also called R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, is a competitive inhibitor of SAP binding to amyloid fibrils. CPHPC is a [[proline]]-derived small palindromic molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating [[serum amyloid protein]] (SAP). It also crosslinks and dimerizes SAP, which is cleared rapidly by the [[liver]]. The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for [[amyloidosis]].<ref name="pmid12015594">{{cite journal| author = Pepys MB, Herbert J, Hutchinson WL, Tennent GA, Lachmann HJ, Gallimore JR, Lovat LB, Bartfai T, Alanine A, Hertel C, Hoffmann T, Jakob-Roetne R, Norcross RD, Kemp JA, Yamamura K, Suzuki M, Taylor GW, Murray S, Thompson D, Purvis A, Kolstoe S, Wood SP, Hawkins PN | title = Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis | journal = Nature | volume = 417 | issue = 6886 | pages = 254–9 | year = 2002 | pmid = 12015594 | doi = 10.1038/417254a }}</ref>
CPHPC, also called R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, is a competitive inhibitor of SAP binding to amyloid fibrils. CPHPC is a [[proline]]-derived small palindromic molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating [[serum amyloid protein]] (SAP). It also crosslinks and dimerizes SAP, which is cleared rapidly by the [[liver]]. The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for [[amyloidosis]].


==References==
==References==

Revision as of 18:24, 12 May 2013

Cardiac amyloidosis Microchapters

Home

Patient Information

Overview

Historical Perspective

Classification

Pathophysiology

Causes

Differentiating Cardiac Amyloidosis from other Diseases

Epidemiology and Demographics

Risk Factors

Screening

Natural History, Complications and Prognosis

Diagnosis

Diagnostic Study of Choice

History and Symptoms

Physical Examination

Laboratory Findings

Electrocardiogram

X-ray

Echocardiography and Ultrasound

CT scan

MRI

Other Imaging Findings

Other Diagnostic Studies

Treatment

Medical Therapy

Surgery

Primary Prevention

Secondary Prevention

Cost-Effectiveness of Therapy

Future or Investigational Therapies

Case Studies

Case #1

Cardiac amyloidosis future or investigational therapies On the Web

Most recent articles

Most cited articles

Review articles

CME Programs

Powerpoint slides

Images

American Roentgen Ray Society Images of Cardiac amyloidosis future or investigational therapies

All Images
X-rays
Echo & Ultrasound
CT Images
MRI

Ongoing Trials at Clinical Trials.gov

US National Guidelines Clearinghouse

NICE Guidance

FDA on Cardiac amyloidosis future or investigational therapies

CDC onCardiac amyloidosis future or investigational therapies

Cardiac amyloidosis future or investigational therapies in the news

Blogs on Cardiac amyloidosis future or investigational therapies

Directions to Hospitals Treating Cardiac amyloidosis

Risk calculators and risk factors for Cardiac amyloidosis future or investigational therapies

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Raviteja Guddeti, M.B.B.S. [2]; Aarti Narayan, M.B.B.S [3]

Overview

New therapies targeting the serum amyloid protein (SAP), which is an excellent immunogen and a universal component of all amyloid deposits, using monoclonal antibodies are currently being investigated.

Future and Investigational Therapies

Possible future treatment options which are currently being investigated include:

  • Anti-SAP antibody
  • CPHPC[1]
  • Diflunisal[2]
  • Tamafidis[3]
  • Eprodisate

CPHPC, also called R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, is a competitive inhibitor of SAP binding to amyloid fibrils. CPHPC is a proline-derived small palindromic molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating serum amyloid protein (SAP). It also crosslinks and dimerizes SAP, which is cleared rapidly by the liver. The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for amyloidosis.

References

  1. Pepys MB, Herbert J, Hutchinson WL, Tennent GA, Lachmann HJ, Gallimore JR, Lovat LB, Bartfai T, Alanine A, Hertel C, Hoffmann T, Jakob-Roetne R, Norcross RD, Kemp JA, Yamamura K, Suzuki M, Taylor GW, Murray S, Thompson D, Purvis A, Kolstoe S, Wood SP, Hawkins PN (2002). "Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis". Nature. 417 (6886): 254–9. doi:10.1038/417254a. PMID 12015594.
  2. Sekijima Y, Dendle MA, Kelly JW (2006). "Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis". Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 13 (4): 236–49. doi:10.1080/13506120600960882. PMID 17107884. Unknown parameter |month= ignored (help)
  3. Bulawa CE, Connelly S, Devit M; et al. (2012). "Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade". Proceedings of the National Academy of Sciences of the United States of America. 109 (24): 9629–34. doi:10.1073/pnas.1121005109. PMC 3386102. PMID 22645360. Unknown parameter |month= ignored (help)


Template:WikiDoc Sources