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provides coniferyl ferulate(CAS#:6691-83-4) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
The prospective multi-center ACRIN 6691 trial was designed to evaluate whether changes from baseline to mid-therapy in a Diffuse Optical Spectroscopic Imaging (DOSI)-derived imaging endpoint, the Tissue Optical Index (TOI), predict pathologic complete response (pCR) in women undergoing breast cancer neoadjuvant chemotherapy (NAC). DOSI instruments were constructed at the University of California, Irvine and delivered to 6 institutions where 60 subjects with newly-diagnosed breast tumors (at least 2 cm in the longest dimension) were enrolled over a 2-year period. Bedside DOSI images of the tissue concentrations of deoxy-hemoglobin (ctHHb), oxy-hemoglobin (ctHbO2), water (ctH2O), lipid, and TOI (ctHHb × ctH2O/lipid) were acquired on both breasts up to 4 times during NAC treatment: baseline, one-week, mid-point, and completion. Of the 34 subjects (mean age 48.4 ± 10.7 years) with complete, evaluable data from both normal and tumor-containing breast, 10 (29%) achieved pCR as determined by central pathology review. The percent change in tumor to normal TOI ratio (%TOITN) from baseline to mid-therapy ranged from −82% to 321%, with a median of −36%. Using pCR as the reference standard and receiver-operating characteristic curve methodology, %TOITN AUC was 0.60 (95% CI 0.39 to 0.81). In the cohort of 17 patients with baseline tumor oxygen saturation (%StO2) greater than the 77% population median, %TOITN AUC improved to 0.83 (95% CI 0.63 to 1.00). We conclude that the combination of baseline functional properties and dynamic optical response shows promise for clinical outcome prediction.
Functional imaging, metabolic imaging, near infrared spectroscopy, breast cancer, neoadjuvant chemotherapy
Predicting Responses to Neoadjuvant Chemotherapy in Breast Cancer: ACRIN 6691 Trial of Diffuse Optical Spectroscopic Imaging (DOSI)
Bruce J. Tromberg,1,* Zheng Zhang,2 Anaïs Leproux,1 Thomas D. O’Sullivan,1 Albert E. Cerussi,1 Philip Carpenter,3 Rita S. Mehta,4 Darren Roblyer,5 Wei Yang,6 Keith D. Paulsen,7 Brian W. Pogue,7 Shudong Jiang,7 Peter Kaufman,8 Arjun G. Yodh AG,9 So Hyun Chung,9 Mitchell Schnall,10 Bradley S. Snyder,11 Nola Hylton,12 David A. Boas,13 Stefan A. Carp,13 Steven J. Isakoff,14 and David Mankoff15, on behalf of the ACRIN 6691 investigators
2017 Oct 15.
By using reverse transcriptase/PCR and oligonucleotide sequences derived from conserved segments (including the conserved RRGDL sequence) of the known proprotein convertases (PCs) PC1, PC2, furin, and PC4, we identified a subtilisin/kexin-like PC called PC5 in both mouse and rat tissues. The composite structure (2.85 kb) was deduced from the analysis of the reverse transcription/PCR products combined with the sequence from a clone isolated from a cDNA library made from corticotropin-activated mouse adrenocortical Y1 cells. The deduced cDNA structures of mouse PC5 and rat PC5 showed that the closest homologue is PACE4. Furthermore, like furin, Drosophila melanogaster (d) dfurin2, and PACE4, PC5 shows the presence of a C-terminal Cys-rich domain containing either 5 (PC5 and PACE4) or 10 (dfurin2) repeats of the consensus motif Cys-Xaa2-Cys-Xaa3-Cys-Xaa(5-7)-Cys-Xaa2-Cys-Xaa (8-15)-Cys-Xaa3-Cys-Xaa(9-16). The richest sources of rat PC5 mRNA (3.8 kb) are the adrenal and gut, but it can also be detected in many endocrine and nonendocrine tissues. Corticotropin-stimulated adrenocortical Y1 cells showed an increased expression of PC5 mRNA, suggesting an upregulation by cAMP. In situ hybridization of rat brain sections demonstrated a unique distribution of PC5 compared to PC1, PC2, and furin.
cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells.
J Lusson, D Vieau, J Hamelin, R Day, M Chretien, and N G Seidah
1993 Jul 15
When the isolated D1/D2/cytochrome b559 complex was exposed to bright light, a distinctive pattern of D1 polypeptide fragments was observed under both aerobic and anaerobic conditions. The major degradation product had an apparent molecular mass of 24 kDa, while other fragments were detected at 17, 14, and 10 kDa by immunoblotting. This pattern was observed when the electron acceptors 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone or silicomolybdate were present during illumination. It is known that these conditions stabilize P680+ chlorophyll and bring about the photooxidation and destruction of pigments in the reaction center, particularly chlorophyll absorbing at 670 nm and beta-carotene. When P680+ was not allowed to accumulate, either by omission of an electron acceptor or by addition of both an electron donor (Mn2+) and an acceptor, no breakdown fragments were observed. In the former case, however, some degradation of the D1 and D2 polypeptides did occur. Under conditions that gave rise to the characteristic D1 breakdown pattern, the D2 polypeptide was also degraded to specific fragments detected at about 29 and 21 kDa by immunoblotting. The results indicate that the photoinduced degradation of D1 (and D2) does not involve exogenous proteases but is most likely an autoproteolytic process. Moreover, our data indicate that the photochemical damage giving rise to D1 and D2 degradation occurs on the oxidizing rather than the reducing side of photosystem II and involves photooxidation of the accessory pigments. The results are discussed in terms of D1 and D2 turnover and photoinhibition.
Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem.
C A Shipton and J Barber
1991 Aug 1;