127869-51-6 Usage
Description
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT), also known as Natriuretic Peptide, C-Type (NPPC/ CNP), is a 22 amino acid peptide encoded by the NPPC gene. It is a part of the natriuretic peptide family, characterized by the absence of C-terminal tail extensions from the intramolecular ring. This peptide is highly expressed in the brain, vascular endothelial cells, and chondrocytes of mammals, where it acts as a paracrine/autocrine factor.
Uses
1. Used in Pharmaceutical Industry:
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT) is used as a therapeutic agent for various cardiovascular and metabolic disorders. It helps in regulating blood pressure, blood volume, and electrolyte balance, as well as promoting the growth and differentiation of cells.
2. Used in Research and Development:
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT) is used as a research tool for studying the biological functions and mechanisms of the natriuretic peptide family. It aids in understanding the role of CNP in various physiological processes and its potential as a therapeutic target for different diseases.
3. Used in Diagnostic Applications:
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT) can be used as a diagnostic marker for detecting and monitoring certain cardiovascular and metabolic conditions. Its levels in blood or other biological samples can provide valuable information about the patient's health status and the effectiveness of treatment.
4. Used in Drug Development:
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT) serves as a lead compound for the development of new drugs targeting the natriuretic peptide system. Researchers can use this peptide to design and synthesize novel agonists and antagonists with improved pharmacological properties and therapeutic potential.
5. Used in Cell Culture and Tissue Engineering:
C-TYPE NATRIURETIC PEPTIDE (32-53) (HUMAN, PORCINE, RAT) can be used in cell culture and tissue engineering applications to promote cell growth, differentiation, and tissue regeneration. It can be incorporated into biomaterials and scaffolds to enhance their bioactivity and support the growth of various cell types.
Properties
The Mr of mature human CNP is 2199, and pI is about
9. It is soluble in water, acid, and 67% acetone, and partially soluble in 99% acetone. However, CNPs are not as
soluble in water as other NPs because of higher hydrophobicity. A CNP solution in water at >10-4M is stable
for more than a year at -20°C.
Gene, mRNA, and precursor
The human CNP gene (NPPC) is located on chromosome 2 (2q37.1), which is different from the loci of the
atrial natriuretic peptide (ANP) and B-type natriuretic
peptide (BNP) genes (NPPA and NPPB, 1p36). The
mouse CNP gene (Nppc) is on chromosome 1. In addition
to the mammalian CNP, all four types of CNP genes in
teleosts are composed of three exons and two introns,
although the exon-intron arrangement between CNP1/
2 and CNP3/4 is different. In elasmobranchs and cyclostomes, only one intron has been found in their nppc. The
human CNP mRNA is 1055 bp in length (381 bp coding
sequence). The human proCNP1–103 is cleaved into
CNP-53 (CNP51–103) and N-terminal (NT)-proCNP1–50
by the prohormone convertase furin.CNP-53 is further processed to give rise to the bioactive
mature form CNP-22 and inactive NT-CNP-53.
Distribution of mRNA
CNPs are highly expressed in the brains of tetrapods. In mammals, CNP transcripts are also identified in the
pituitary, cardiovascular system, endochondral bone,?and reproductive systems.6 In teleosts, CNP1, CNP2, and
CNP4 are predominantly expressed in the brain, whereas
CNP3 is expressed in a variety of tissues including the
heart, pituitary, kidney, spleen, ovary, spinal cord, and
intestine. In elasmobranchs and cyclostomes, where
only a single CNP but no cardiac ANP/BNP/ventricular
natriuretic peptide (VNP) is found, CNP mRNA is
strongly expressed in both the brain and the heart. It
is noteworthy that CNP acts both as an endocrine hormone and as a paracrine/autocrine factor in these primitive vertebrates.
Synthesis and release
The human NPPC and mouse Nppc have a Y-box, a
CRE-like sequence, and a GC box in the proximal
50
-flanking region (the NF-κB recognition site is present
only in mouse Nppc). The putative transcription factors
are Sp-1, CREB, TSC22D1, and STK16. The regulation
of CNP release has been extensively studied using cultured endothelial cells, and CNP secretion is enhanced
by TGF-β, TNF-α, IL-1, ANP, and sheer stress, and suppressed by insulin and VEGF. Unlike ANP, CNPs are
not stored in large secretory granules.
Receptors
The functional receptor for CNPs is the B-type NP
receptor (NPR-B or GC-B, Kd =30 pM). Similarly to the
receptor for ANP/BNP (NPR-A or GC-A), NPR-B is
coupled with guanylyl cyclase, which is involved in the?cGMP-mediated intracellular signaling cascade, and
forms a homotetramer. In the medaka, CNP1, 2, and 4
bind to OlGC1 (a NPR-B homolog) while CNP3 prefers
OlGC2 (one of two NPR-A homologs). The human
NPR-B gene (NPR2) is located on chromosome 9
(9p13.3) and its protein contains 1047 aa residues with
an Mr of 117,022. NPR2 is widely expressed throughout
the body, including the brain, chondrocytes, lung, vascular smooth muscle, adrenal, kidney, ovary, and uterus. In the shark, npr2 is expressed in the rectal gland, a distinct salt-secreting organ. In the rainbow trout, the
expression of npr2 decreased upon transfer to seawater. CNPs also bind to the guanylyl cyclase-deficient receptor,
C-type NP receptor (NPR-C/NPR3), with high affinity
(Kd=48 pM).
Biological functions
CNPs do not induce natriuresis at physiological concentrations. In mammals, the most recognized function
of CNP is the regulation of long bone growth. CNP targets chondrocytes to promote endochondral ossification.
CNP also has a vasodepressor effect in mammals, teleosts
(the eel and trout) and elasmobranchs, presumably
through its action on the vascular smooth muscle. In the medaka that lack npr1, CNP3 appears to be important for normal atrial development, as CNP3 knockdown
resulted in the hypertrophy of the atrium. Thus, CNP3
appears to take over the roles of ANP in this teleost. In the
shark, CNP3 stimulates the release of vasoactive intestinal peptide (VIP) from the nerve terminals within the rectal gland.
Biochem/physiol Actions
C-type natriuretic peptide is produced in the hypothalamus, anterior pituitary, and most major endocrine glands. It has potent venodilatory and coronary vasodilatory effects, but minimal effects on renal function.
Clinical Use
CNP has not been used as a diagnostic or therapeutic
tool. Several studies suggested potential uses of CNP,
such as for the treatment for growth disorders and as a
biomarker of growth plate activity.
Structure and conformation
Human proCNP consists of 103 aa residues with a bioactive mature CNP at the C-terminus. All
four types of CNPs consist of 22 aa residues except for
some teleost CNP4. Like other NPs, CNPs have a
17 aa intramolecular ring, but lack a C-terminal tail
sequence. CNPs are the most conserved NPs, although they contain different groups of peptides. The sequence identity
of mature CNP4 is >95% in mammals, except for unique
CNP in the little brown bat (Myotis lucifugus). CNP1 and
CNP3 are also well conserved (both >80% identity) in
each vertebrate class that possesses both peptides. In
contrast, CNP2 in teleosts is not so conserved. Although
major CNPs are of different types among vertebrate classes, mature sequences are highly conserved among these
CNPs, suggesting that CNPs have undergone
convergent evolution.
Check Digit Verification of cas no
The CAS Registry Mumber 127869-51-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,7,8,6 and 9 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 127869-51:
(8*1)+(7*2)+(6*7)+(5*8)+(4*6)+(3*9)+(2*5)+(1*1)=166
166 % 10 = 6
So 127869-51-6 is a valid CAS Registry Number.
127869-51-6Relevant articles and documents
Epimerization-Free Preparation of C-Terminal Cys Peptide Acid by Fmoc SPPS Using Pseudoproline-Type Protecting Group
Tsuda, Shugo,Masuda, Shun,Yoshiya, Taku
, p. 1674 - 1679 (2020)
Preparation of C-terminal Cys-containing peptide acid by Fmoc solid-phase peptide synthesis (SPPS) is difficult due to base-mediated epimerization at Cys. In this paper, use of a C-terminal pseudoproline structure and Trt(2-Cl) resin achieved epimerization-free direct preparation of the C-terminal Cys-containing peptide acid by Fmoc SPPS. Additionally, the C-terminal Cys(ψDmp,Hpro)-containing protected peptide segment was applied to an epimerization-free segment condensation reaction.
